Notice of Pre-AIA or AIA Status The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. DETAILED ACTION This application is a 371 of PCT/EP2021/070696. The response filed on September 24, 2025 has been entered. Election /Restrictions Applicant’s election of Group I with a specie election of ( 1) B. licheniformis as the bacterial cell, (2) alr (of B. licheniformis ) as the first inactivated alanine racemase gene and yncD of ( B. licheniformis ) as the second inactivated alanine racemase gene , and (3) plasmid pUKAS58P (including the alrA gene from B. subtilis with its nativ e promoter region (SEQ ID NO: 5) and the promoter of the aprE gene from B. licheniformis from pCB56C, and the protease gene of pCB56C , Example 2, in the reply filed on September 24, 2025 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Claims 12-19 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on September 24, 2025. Status of Claims Claims 1-19 are pending. Claims 12-19 are withdrawn. Claims 1-11 are under examination. Foreign Priority Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Information Disclosure Statement The information disclosure statement (IDS) submitted o n June 7, 2023 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Claim Objections Clai ms 5 and 9 are objected to because of the following informalities: The microorganisms “ Bacillus licheniformis” and “B. subtilis” should be italicized. Appropriate correction is required . Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(b): (b ) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the appl icant regards as his invention. Claim 1 and claims 2-11 depending therefrom are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 1 r ecite s the limitation s “ maintaining said plasmid” . The metes and bounds of the limitation in the context of the above claim are not clear . It is unclear what aspects of the plasmid is maintained. Clarification is requested. The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. Claims 1- 4 and 6-11 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. MPEP 2111.01 states that ''[d] uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The claims have been broadly interpreted to encompass a method of producing a polypeptide of interest in any bacterial host cell or any Bacilli host cell by inactivating a first and second chromosomal gene encoding a first and second alanine racemase and providing a plasmid comprising an autonomous replication sequence, polynucleotide encoding a polypeptide of interest, and a polynucleotide encoding a third alanine racemase. Therefore, the claims are drawn to a method of producing a polypeptide of interest in a genus of bacterial host cell or Bacilli host cell by inactivating a genus of first and second chromosomal gene encoding a first and second alanine racemase. MPEP 2163 I. states that to “ satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention. According to MPEP 2163.II.A.3.(a).ii), “S atisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’" The recitations of “bacterial host cell”, “Bacilli” host cell, “ first chromosomal gene encoding a first alanine racemase”, and “ second chromosomal gene encoding a second alanine racemase” fail to provide a sufficient description of the genus of the host cells used in the claimed method as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus. The prior art discloses a method of producing a polypeptide of interest in a Bacillus subtilis host cel l by inactivating its chromosomal genes encoding two alanine racemases ( alr and yncD ) , see Lenhard ( WO 2010/020589 – form PTO-1449). However, in activation of two alanine racemase genes in any bacterial host cell and in any Bacilli host cell was not known in the prior art. The specification is limited to a method of produci ng a polypeptide of interest in Bacillus licheniformis and Bacillus subtilis b y inactivating its first and second chromosomal gene encoding a first and second alanine racemase . While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or inventions in an unpredictable art, adequate written description of a genus w hich embraces widel y variant species cannot be achieved by disclosing only one species within the genus.” In view of the widely variant species encompassed by the genus, the two examples escribed above are not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus. T he claimed invention requires a defined set of host cells and a first and second chromosomal gene encoding a first and second alanine racemase . Although the specification discloses exemplary host cells and a first and second chromosomal gene encoding a first and second alanine racemase , a “laundry list” disclosure of every possible moiety does not necessarily constitute a written description of every species in a genus because it would not “reasonably lead” those skilled in the art to any particular species, see Fujikawa v. Wattanasin , 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) or MPEP 2163. While the exemplary host cells and a first and second chromosomal gene encoding a first and second alanine racemase were known in the art, this knowledge alone would not allow one level of skill in the art to immediately envisage the claimed genus . Therefore, the level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which host cells to use in the claimed method . Given this lack of description of the representative species enco mpassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 1- 4 and 6-11 . Claim Rejections - 35 USC § 102 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis ( i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale , or otherwise available to the public before the effective filing date of the claimed invention. Claim(s) 1-4 and 6-1 0 is/are rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Lenhard ( WO 2010/020589 – form PTO-1449) . Regarding claim s 1 - 4 , Lenhard discloses a method of producing a polypeptide of interest (abstract) by a 1 ) providing a Bacillus subtilis host cell , which belongs to Firmicutes ( page 12, lines 24-29) , comprising a first chromosomal gene encoding a first d- alanine racemase (air, also known as alr ) and a second chromosomal gene encoding a second d- alanine racemase ( YncD ) , a2) inactivating said first and second chromosomal genes by mutation (abstract, page 3, lines 7-19, page 14, lines 1-27, and Examples 1-3), and a3) introducing in to said host cell a plasmid comprising 1 . an autonomous replication sequence (page 18, lines 27-31), 2 . p oly nucleotide encoding a polypeptide of interest operably linked to a promoter (page 14, lines 30-35, page 18, lines 27-31) , and 3 . a polynucleotide encoding a third alanine racemase operably linked to a promoter (Example 3 and Figure 4 ) , and b) cultivating the host cells under conditions for maintaining the plasmid in the host cell and expressing said polypeptide of interest and producing said polypeptide of interest (page 14, lines 30-35). Regarding claim 6, the plasmid of Lenhard comprises a polynucleotide encoding a polypeptide of interest is heterologous to the bacterial cell (Example 2) . Regarding claim 7, the third alanine racemase (air, UNIPROT:P10725) has 100% sequence identity to the alanine racemase ( alrA ) of SEQ ID NO:4 of the instant application (page 13, lines 32-37 and see the sequence alignment below). Regarding claim 8, Lenhard discloses using various promoters, including constitutive promoter XylA (page 15, lines 11-21). Regarding claim 9, since the polynucleotide encoding the third B. subtilis alanine racemase gene is intact, said third alanine racemase is linked to the promoter of the B. subtilis alanine racemase (Example 3). Regarding claim 10, Lenhard discloses that the polypeptide of interest is an enzyme , such as a protease (page 17, lines 4-13), operably linked to a promoter from aprE (page 16, lines 19-27). Therefore, the reference Lenhard anticipates claims 1-4 and 6-10. Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness . This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claim (s) 1-11 s/are rejected under 35 U.S.C. 103 as being unpatentable over Lenhard ( WO 2010/020589 – form PTO-1449) and Salifu ( Cloning and analysis of two alanine racemase genes from Bacillus licheniformis . Ann. Microbiol . 58 , 287–291 (2008) – form PTO-1449) and evidenced by D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892). Regarding claims 1-4, Lenhard discloses a method of producing a polypeptide of interest (abstract) by a 1 ) providing a Bacillus subtilis host cell, which belongs to Firmicutes (page 12, lines 24-29) comprising a first chromosomal gene encoding a first d-alanine racemase (air, also known as alr ) and a second chromosomal gene encoding a second d-alanine racemase ( YncD ), a2) inactivating said first and second chromosomal genes by mutation (abstract, page 3, lines 7-19, page 14, lines 1-27, and Examples 1-3), and a3) introducing in to said host cell a plasmid comprising 1 . an autonomous replication sequence (page 18, lines 27-31), 2 . polynucleotide encoding a polypeptide of interest operably linked to a promoter (page 14, lines 30-35, page 18, lines 27-31), and 3 . a polynucleotide encoding a third alanine racemase operably linked to a promoter (Example 3 and Figure 4), and b) cultivating the host cells under conditions for maintaining the plasmid in the host cell and expressing said polypeptide of interest and producing said polypeptide of interest (page 14, lines 30-35). Regarding claim 6, the plasmid of Lenhard comprises a polynucleotide encoding a polypeptide of interest is heterologous to the bacterial cell (Example 2). Regarding claim 7, the third alanine racemase (air, UNIPROT:P10725) has 100% sequence identity to the alanine racemase ( alrA ) of SEQ ID NO:4 of the instant application (page 13, lines 32-37 and see the sequence alignment below). Regarding claim 8, Lenhard discloses using various promoters, including constitutive promoter XylA (page 15, lines 11-21). Regarding claim 9, since the polynucleotide encoding the third B. subtilis alanine racemase gene is intact, said third alanine racemase is linked to the promoter of the B. subtilis alanine racemase (Example 3). Regarding claim 10, Lenhard discloses that the polypeptide of interest is an enzyme (page 17, lines 4-13). Regarding claim 5, Lenhard discloses that the preferred host cell is Bacillus subtilis or Bacillus licheniformis (page 12, lines 27-29). Lenhard discloses that using D -alanine racemase deficient host cells together with D -alanine free growth medium and a transformation polynucleotide construct that complements the deficiency (via expression of an alanine racemase) , provides a way to dramatically improve the efficiency of expression of genes without the need to use antibiotics (page 2, last paragraph). However, Lenhard does not disclose a Bacillus licheniformis alanine racemase alr and yncD . Salifu discloses that Bacillus licheniformis has been widely used for the production of enzymes (page 287, 1 st paragraph). Salifu discloses that because alanine racemase activity is essential for bacterial growth, it has been exploited in the development of a positive selection system for plasmid maintenance ( page 287, 2 nd paragraph). Salifu discloses two Bacillus licheniformis alanine racemases, Alr and Alr2 (page 288, last paragraph). Salifu discloses that alanine racemases Alr is designated as YP_077790 (replaced by WP_011197569.1 , see page 1 of D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892), which has 100% sequence identity to the Bacillus licheniformis alr of SEQ ID NO:2 of the instant application (see FIG. 1 and see the sequence alignment below). Salifu discloses that alanine racemases Alr 2 is designated as YP_080385 (replaced by WP_003184708.1 , see page 2 of D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892), which has 100% sequence identity to the Bacillus licheniformis yncD of SEQ ID NO:2 5 of the instant application (see FIG. 1 and see the sequence alignment below). Therefore, in combining the teachings of the above references , it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the method of Lenhard by substituting the Bacillus subtilis host cell with Bacillus licheniformis and inactivate the Bacillus licheniformis alr and alr2 ( yncD ) and further isolate and purify the polypeptide of interest . One having ordinary skill in the art would have been motivated to do so in order to produce a polypeptide of interest in Bacillus licheniformis in a positive selection system since Bacillus licheniformis is widely used to produce enzymes of interest and Lenhard discloses that Bacillus licheniformis is a preferred host cell. One having ordinary skill in the art would have had a reasonable expectation of success at arriving at the claimed invention because Lenhard discloses a method of producing a polypeptide of interest in a Bacillus subtilis host cell comprising inactivated two alanine racemases and expressing a polynucleotide encoding an alanine racemase and a polynucleotide encoding a polypeptide of interest, Lenhard discloses that Bacillus licheniformis is a preferred host cell, Salifu discloses Bacillus licheniformis is widely used as for the production of enzymes, and Salifu discloses Bacillus licheniformis alanine racemase alr and yncD . T he rationale to support a conclusion that the claims would have been obvious is that the substitution of one known element ( Bacillus subtilis host cel l ) for another yields predictable results ( Bacillus licheniformis host cell ) to one of ordinary skill in the art. Therefore, it would have been obvious to one of ordinary skill in the art to replace the prior art Bacillus subtilis host cell with another known and available Bacillus host cell , such as B. licheniformis . Therefore, the above references render claims 1-11 prima facie obvious. Double Patenting The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg , 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman , 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi , 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum , 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel , 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington , 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA/25, or PTO/AIA/26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer . Claims 1-11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of copending Application No. 18/017,426 (reference application) in view of Salifu ( Cloning and analysis of two alanine racemase genes from Bacillus licheniformis . Ann. Microbiol . 58 , 287–291 (2008) – form PTO-1449) and evidenced by D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892) . Although the claims at issue are not identical, they are not patentably distinct from each other because they are claiming common subject matter, as follows: The claims of the instant application and the claims of t he reference application are directed to a method of producing a polypeptide of interest in Bacillus licheniformis. Regarding claims 1- 6 of the instant application, claim s 1 -3 of the reference application recites a method of producing a polypeptide of interest by a 1 ) providing a Bacillus licheniformis host cell comprising a c hromosomal gene encoding a lr , a2) inactivating said alrgene by mutation , and a3) introducing in to said host cell a plasmid comprising 1 . an autonomous replication sequence , 2 . polynucleotide encoding a polypeptide of interest operably linked to a promoter , and 3 . a polynucleotide encoding an alanine racemase not native to the host cell operably linked to a promoter, and b) cultivating the host cells under conditions for maintaining the plasmid in the host cell and expressing said polypeptide of interest and producing said polypeptide of interest . Therefore, claims 1-6 of the instant application are anticipated by claims 1-3 of the reference application. Regarding claim 7 of the instant application , claim 7 of the reference application recites that the a lanine racemase not native to the host cell has at least 40- 100% sequence identity to the alanine racemase of SEQ ID NO:4 . SEQ ID NO:4 of the instant application is identical to SEQ ID NO:4 of the reference application. Therefore, claim 7 of the instant application is anticipated by claim 7 of the reference application. Regarding claim 8 of the instant application , claim 9 recites that the promoter linked to the alanine racemase is a constitutive promoter . Therefore, claim 8 of the instant application is anticipated by claim 9 of the reference application. Regarding claim 9 of the instant application , claim 10 of the reference application recites that the promoter linked to the alanine racemase is the promoter of the B. subtilis alrA gene. Therefore, claim 9 of the instant application is anticipated by claim 10 of the reference application. Regarding claim 10 of the instant application , claim 12 of the reference application recites that the polypeptide of interest is an enzyme. Therefore, claim 10 of the instant application is anticipated by claim 12 of the reference application. Regarding claim 11 of the instant application, claim 15 of the reference application recites purifying the polypeptide of interest. Therefore, claim 11 of the instant application is anticipated by claim 15 of the reference application. However, the claims of the reference application do not recite inactivating a second alanine racemase gene , yncD . Salifu discloses that Bacillus licheniformis has been widely used for the production of enzymes (page 287, 1 st paragraph). Salifu discloses that because alanine racemase activity is essential for bacterial growth, it has been exploited in the development of a positive selection system for plasmid maintenance (page 287, 2 nd paragraph). Salifu discloses two Bacillus licheniformis alanine racemases, Alr and Alr2 (page 288, last paragraph). Salifu discloses that alanine racemases Alr is designated as YP_077790 (replaced by WP_011197569.1 , see page 1 of D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892), which has 100% sequence identity to the Bacillus licheniformis alr of SEQ ID NO:2 of the instant application (see FIG. 1 and see the sequence alignment below). Salifu discloses that alanine racemases Alr 2 is designated as YP_080385 (replaced by WP_003184708.1 , see page 2 of D-alanine racemase [ Bacillus licheniformis DSM 13 = ATCC 14580. Retrieved on December 16, 2025 – form PTO-892), which has 100% sequence identity to the Bacillus licheniformis yncD of SEQ ID NO:25 of the instant application (see FIG. 1 and see the sequence alignment below). Therefore, it would have been obvious to one having ordinary skill in the art to modify the claims of the reference application by inactivating the second alanine racemase gene, yncD , in the Bacillus licheniformis host cell of the reference application . One having ordinary skill in the art would have been motivated to do so in order to inactivate all alanine racemase genes in Bacillus licheniformis in order to achieve a positive selection system . One having ordinary skill in the art would have had a reasonable expectation of success at arriving at the claimed invention because the claims of the reference application discloses a method of producing a polypeptide of interest in a Bacillus licheniformis host cell comprising an i nactivated alanine racemase and expressing a polynucleotide encoding an alanine racemase and a polynucleotide encoding a polypeptide of interest and Salifu discloses Bacillus licheniformis alanine racemase alr and yncD . Therefore, the conflicting claims are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Conclusion Claims 1-19 are pending. Claims 12-19 are withdrawn. Claims 1-11 are rejected. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT YONG D PAK whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-0935 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-Th: 5:30 am - 3:30 pm . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Robert Mondesi can be reached on FILLIN "SPE Phone?" \* MERGEFORMAT 408-918-7584 . The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /YONG D PAK/ Primary Examiner, Art Unit 1652 Sequence alignment of Bacillus subtilis alanine racemase of SEQ ID NO: 4 of the instant application (“ Qy ”) and Bacillus subtilis alanine racemase (air) of Lenhard (“D b ”) ALR1_BACSU ID ALR1_BACSU Reviewed; 389 AA. AC P10725 ; P96620; DT 01-JUL-1989, integrated into UniProtKB /Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 18-JUN-2025, entry version 161. DE RecName : Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201}; GN Name=alr1; Synonyms= alr , dal; OrderedLocusNames =BSU04640; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillati ; Bacillota ; Bacilli; Bacillales ; Bacillaceae ; Bacillus. OX NCBI_TaxID =224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Ferrari E., Henner D.J., Yang M.Y.; RT "Isolation of an alanine racemase gene from Bacillus subtilis and its use RT for plasmid maintenance in B. subtilis."; RL Biotechnology (N.Y.) 3:1003-1007(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.; RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus RT subtilis genome."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr -Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May CC also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine = D-alanine; Xref =Rhea:RHEA:20249, CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref =ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16207; AAA22378.1; -; Genomic_DNA . DR EMBL; AB001488; BAA19301.1; -; Genomic_DNA . DR EMBL; AL009126; CAB12271.1; -; Genomic_DNA . DR PIR; JS0443; JS0443. DR RefSeq ; WP_003234284.1; NZ_OZ025638.1. DR AlphaFoldDB ; P10725; -. DR SMR; P10725; -. DR FunCoup ; P10725; 386. DR STRING; 224308.BSU04640; -. DR jPOST ; P10725; -. DR PaxDb ; 224308-BSU04640; -. DR EnsemblBacteria ; CAB12271; CAB12271; BSU_04640. DR GeneID ; 939942; -. DR KEGG; bsu:BSU04640; -. DR PATRIC; fig|224308.179.peg.492; -. DR eggNOG ; COG0787; Bacteria. DR InParanoid ; P10725; -. DR OrthoDB ; 9813814at2; -. DR PhylomeDB ; P10725; -. DR BioCyc ; BSUB:BSU04640-MONOMER; -. DR BRENDA; 5.1.1.1; 658. DR SABIO-RK; P10725; -. DR UniPathway ; UPA00042; UER00497. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central . DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central . DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central . DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central . DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central . DR CDD; cd00430; PLPDE_III_AR; 1. DR FunFam ; 2.40.37.10:FF:000006; Alanine racemase; 1. DR FunFam ; 3.20.20.10:FF:000002; Alanine racemase; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 1. DR HAMAP; MF_01201; Ala_racemase ; 1. DR InterPro ; IPR000821; Ala_racemase . DR InterPro ; IPR009006; Ala_racemase / Decarboxylase_C . DR InterPro ; IPR011079; Ala_racemase_C . DR InterPro ; IPR001608; Ala_racemase_N . DR InterPro ; IPR020622; Ala_racemase_pyridoxalP -BS. DR InterPro ; IPR029066; PLP- binding_barrel . DR NCBIfam ; TIGR00492; alr ; 1. DR PANTHER; PTHR30511; ALANINE RACEMASE; 1. DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1. DR Pfam ; PF00842; Ala_racemase_C ; 1. DR Pfam ; PF01168; Ala_racemase_N ; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C ; 1. DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 3: Inferred from homology; KW Isomerase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1..389 FT /note="Alanine racemase 1" FT /id="PRO_0000114500" FT ACT_SITE 41 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT ACT_SITE 266 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT BINDING 313 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT MOD_RES 41 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201" FT CONFLICT 40 FT /note="V -> E (in Ref. 1; AAA22378)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="V -> M (in Ref. 1; AAA22378)" FT /evidence="ECO:0000305" SQ SEQUENCE 389 AA; 43265 MW; 4802B7C182ACCD58 CRC64; Query Match 100.0%; Score 2009; Length 389; Best Local Similarity 100.0%; Matches 389; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 MSTKPFYRDTWAEIDLSAIKENVSNMKKHIGEHVHLMAVVKANAYGHGDAETAKAALDAG 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MSTKPFYRDTWAEIDLSAIKENVSNMKKHIGEHVHLMAVVKANAYGHGDAETAKAALDAG 60 Qy 61 ASCLAVAILDEAISLRKKGLKAPILVLGAVPPEYVAIAAEYDVTLTGYSVEWLQEAARHT 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ASCLAVAILDEAISLRKKGLKAPILVLGAVPPEYVAIAAEYDVTLTGYSVEWLQEAARHT 120 Qy 121 KKGSLHFHLKVDTGMNRLGVKTEEEVQNVMAILDRNPRLKCKGVFTHFATADEKERGYFL 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 KKGSLHFHLKVDTGMNRLGVKTEEEVQNVMAILDRNPRLKCKGVFTHFATADEKERGYFL 180 Qy 181 MQFERFKELIAPLPLKNLMVHCANSAAGLRLKKGFFNAVRFGIGMYGLRPSADMSDEIPF 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 MQFERFKELIAPLPLKNLMVHCANSAAGLRLKKGFFNAVRFGIGMYGLRPSADMSDEIPF 240 Qy 241 QLRPAFTLHSTLSHVKLIRKGESVSYGAEYTAEKDTWIGTVPVGYADGWLRKLKGTDILV 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 QLRPAFTLHSTLSHVKLIRKGESVSYGAEYTAEKDTWIGTVPVGYADGWLRKLKGTDILV 300 Qy 301 KGKRLKIAGRICMDQFMVELDQEYPPGTKVTLIGRQGDEYISMDEIAGRLETINYEVACT 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 KGKRLKIAGRICMDQFMVELDQEYPPGTKVTLIGRQGDEYISMDEIAGRLETINYEVACT 360 Qy 361 ISSRVPRMFLENGSIMEVRNPLLQVNISN 389 ||||||||||||||||||||||||||||| Db 361 ISSRVPRMFLENGSIMEVRNPLLQVNISN 389 Sequence alignment of Bacillus licheniformis alanine racemase ( alr ) of SEQ ID NO: 2 of the instant application (“ Qy ”) and Bacillus licheniformis alanine racemase ( alr ) of Salifu (“D b ”) Q62YK6_BACLD ID Q62YK6_BACLD Unreviewed; 389 AA. AC Q62YK6; DT 25-OCT-2004, integrated into UniProtKB / TrEMBL . DT 29-MAY-2007, sequence version 2. DT 18-JUN-2025, entry version 139. DE RecName : Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN Name= alr {ECO:0000313|EMBL:AAU22152.2}; GN OrderedLocusNames =BL02201 {ECO:0000313|EMBL:AAU22152.2}; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillati ; Bacillota ; Bacilli; Bacillales ; Bacillaceae ; Bacillus. OX NCBI_TaxID =279010 {ECO:0000313|EMBL:AAU22152.2, ECO:0000313|Proteomes:UP000000606}; RN [1] {ECO:0000313|EMBL:AAU22152.2, ECO:0000313|Proteomes:UP000000606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46 RC {ECO:0000313|Proteomes:UP000000606}; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody- Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine = D-alanine; Xref =Rhea:RHEA:20249, CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00000316, ECO:0000256|HAMAP- CC Rule:MF_01201}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref =ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP- CC Rule:MF_01201}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000002; AAU22152.2; -; Genomic_DNA . DR RefSeq ; WP_011197569.1 ; NC_006322.1. DR AlphaFoldDB ; Q62YK6; -. DR STRING; 279010.BL02201; -. DR GeneID ; 92858489; -. DR KEGG; bli:BL02201; -. DR PATRIC; fig|279010.13.peg.547; -. DR eggNOG ; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_1_9; -. DR UniPathway ; UPA00042; UER00497. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter . DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule . DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule . DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniRule . DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter . DR CDD; cd00430; PLPDE_III_AR; 1. DR FunFam ; 2.40.37.10:FF:000006; Alanine racemase; 1. DR FunFam ; 3.20.20.10:FF:000002; Alanine racemase; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 1. DR HAMAP; MF_01201; Ala_racemase ; 1. DR InterPro ; IPR000821; Ala_racemase . DR InterPro ; IPR009006; Ala_racemase / Decarboxylase_C . DR InterPro ; IPR011079; Ala_racemase_C . DR InterPro ; IPR001608; Ala_racemase_N . DR InterPro ; IPR020622; Ala_racemase_pyridoxalP -BS. DR InterPro ; IPR029066; PLP- binding_barrel . DR NCBIfam ; TIGR00492; alr ; 1. DR PANTHER; PTHR30511; ALANINE RACEMASE; 1. DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1. DR Pfam ; PF00842; Ala_racemase_C ; 1. DR Pfam ; PF01168; Ala_racemase_N ; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C ; 1. DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000000606}. FT DOMAIN 247..372 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 41 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 268 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 315 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 41 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 389 AA; 43612 MW; AF4168FA888E9096 CRC64; Query Match 100.0%; Score 1993; Length 389; Best Local Similarity 100.0%; Matches 389; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 MSLKPFYRKTWAEIDLTALKENVRNMKRHIGEHVRLMAVVKANAYGHGDAQVAKAALAEG 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MSLKPFYRKTWAEIDLTALKENVRNMKRHIGEHVRLMAVVKANAYGHGDAQVAKAALAEG 60 Qy 61 ASILAVALLDEALSLRAQGIEEPILVLGAVPTEYASIAAEKRIIVTGYSVGWLKDVLGFL 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ASILAVALLDEALSLRAQGIEEPILVLGAVPTEYASIAAEKRIIVTGYSVGWLKDVLGFL 120 Qy 121 NEAEAPLEYHLKIDTGMGRLGCKTEEEIKEMMEMTESNDKLNCTGVFTHFATADEKDTDY 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 NEAEAPLEYHLKIDTGMGRLGCKTEEEIKEMMEMTESNDKLNCTGVFTHFATADEKDTDY 180 Qy 181 FNMQLDRFKELISPLPLDRLMVHSSNSAAGLRFREQLFNAVRFGIGMYGLAPSTEIKDEL 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 FNMQLDRFKELISPLPLDRLMVHSSNSAAGLRFREQLFNAVRFGIGMYGLAPSTEIKDEL 240 Qy 241 PFRLREVFSLHTELTHVKKIKKGESVSYGATYTAQRDEWIGTVPVGYADGWLRRLAGTEV 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 PFRLREVFSLHTELTHVKKIKKGESVSYGATYTAQRDEWIGTVPVGYADGWLRRLAGTEV 300 Qy 301 LIDGKRQKIAGRICMDQFMISLAEEYPVGTKVTLIGKQKDEWISVDEIAQNLQTINYEIT 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 LIDGKRQKIAGRICMDQFMISLAEEYPVGTKVTLIGKQKDEWISVDEIAQNLQTINYEIT 360 Qy 361 CMISSRVPRMFLENGSIMEIRNPILPDQS 389 ||||||||||||||||||||||||||||| Db 361 CMISSRVPRMFLENGSIMEIRNPILPDQS 389 Sequence alignment of Bacillus licheniformis alanine racemase ( yncD ) of SEQ ID NO: 25 of the instant application (“ Qy ”) and Bacillus licheniformis alanine racemase ( alr 2) of Salifu (“D b ”) A0A415J6W6_BACLI ID A0A415J6W6_BACLI Unreviewed; 393 AA. AC A0A415J6W6; DT 08-MAY-2019, integrated into UniProtKB / TrEMBL . DT 08-MAY-2019, sequence version 1. DT 18-JUN-2025, entry version 28. DE RecName : Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN Name= alr {ECO:0000313|EMBL:QPR74396.1}; GN ORFNames =CHCC16736_0679 {ECO:0000313|EMBL:TWL31511.1}, I6G80_09060 GN {ECO:0000313|EMBL:QPR74396.1}; OS Bacillus licheniformis. OC Bacteria; Bacillati ; Bacillota ; Bacilli; Bacillales ; Bacillaceae ; Bacillus. OX NCBI_TaxID =1402 {ECO:0000313|EMBL:TWL31511.1, ECO:0000313|Proteomes:UP000435910}; RN [1] {ECO:0000313|EMBL:TWL31511.1, ECO:0000313|Proteomes:UP000435910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAC-16736 {ECO:0000313|EMBL:TWL31511.1, RC ECO:0000313|Proteomes:UP000435910}; RA Wels M., Siezen R.J., Johansen E., Stuer-Lauridsen B., Bjerre K., RA Nielsen B.K.K.; RT "Genome sequence analysis of >100 Bacillus licheniformis strains suggests RT intrinsic resistance to this species."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QPR74396.1, ECO:0000313|Proteomes:UP000595038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_923 {ECO:0000313|EMBL:QPR74396.1, RC ECO:0000313|Proteomes:UP000595038}; RA Nelson B., Plummer A., Tallon L., Sadzewicz L., Zhao X., Boylan J., Ott S., RA Bowen H., Vavikolanu K., Mehta A., Aluvathingal J., Nadendla S., Myers T., RA Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine = D-alanine; Xref =Rhea:RHEA:20249, CC ChEBI:CHEBI:5741