ID   MURI2_BACSU             Reviewed;         265 AA.
AC   O05412;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Glutamate racemase 2 {ECO:0000255|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN   Name=yrpC; OrderedLocusNames=BSU26810;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA   Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA   Duesterhoeft A., Ehrlich S.D.;
RT   "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT   operon reveals two new extracytoplasmic function RNA polymerase sigma
RT   factors SigV and SigZ.";
RL   Microbiology 143:2939-2943(1997).
RN   [2]
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).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10380621; DOI=10.1271/bbb.63.792;
RA   Ashiuchi M., Soda K., Misono H.;
RT   "Characterization of yrpC gene product of Bacillus subtilis IFO 3336 as
RT   glutamate racemase isozyme.";
RL   Biosci. Biotechnol. Biochem. 63:792-798(1999).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR   EMBL; U93875; AAB80890.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14622.1; -; Genomic_DNA.
DR   PIR; C69978; C69978.
DR   RefSeq; NP_390558.1; NC_000964.3.
DR   RefSeq; WP_003229860.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O05412; -.
DR   SMR; O05412; -.
DR   STRING; 224308.BSU26810; -.
DR   PaxDb; O05412; -.
DR   PRIDE; O05412; -.
DR   DNASU; 937619; -.
DR   EnsemblBacteria; CAB14622; CAB14622; BSU_26810.
DR   GeneID; 937619; -.
DR   KEGG; bsu:BSU26810; -.
DR   PATRIC; fig|224308.179.peg.2912; -.
DR   eggNOG; COG0796; Bacteria.
DR   InParanoid; O05412; -.
DR   OMA; KAVMIAC; -.
DR   PhylomeDB; O05412; -.
DR   BioCyc; BSUB:BSU26810-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00258; Glu_racemase; 1.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR   InterPro; IPR004391; Glu_race.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Glutamate racemase 2"
FT                   /id="PRO_0000095454"
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        182
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         183..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   265 AA;  29876 MW;  06F1FE75EBF0AD68 CRC64;
     MKIGFFDSGI GGMTVLYEAI KVLPYEDYIF YADTLNVPYG EKSKGKVKEY IFNAAEFLAS
     QNIKALVIAC NTATSIAIED LRRNFDFPII GIEPAVKPAI NKCTEERKRV LVVATNLTLK
     EEKFHNLVKE IDHHDLVDCL ALPGLVEFAE NFDFSEDKII KYLKNELSSF DLKQYGTIVL
     GCTHFPFFKN SFEKLFGIKV DMISGSVGTA KQLKKVLADR NQLGKGSGSI TFFNSGHKIV
     DQEVISKYKR LFEILDETQR SHVGH