ID   MURL_XANOM              Reviewed;         451 AA.
AC   P0DQD8;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate epimerase {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000305};
DE            EC=5.1.1.23 {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000269|PubMed:28294606};
DE   AltName: Full=UDP-MurNAc-L-Ala-L-Glu epimerase {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000303|PubMed:28294606};
GN   Name=murL {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000303|PubMed:28294606};
GN   OrderedLocusNames=XOO1319 {ECO:0000312|EMBL:BAE68074.1};
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=MAFF 311018;
RX   PubMed=28294606; DOI=10.1021/jacs.7b01221;
RA   Feng R., Satoh Y., Ogasawara Y., Yoshimura T., Dairi T.;
RT   "A glycopeptidyl-glutamate epimerase for bacterial peptidoglycan
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 139:4243-4245(2017).
CC   -!- FUNCTION: Cell wall formation. Catalyzes epimerization of the terminal
CC       L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000269|PubMed:28294606}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate
CC         = AMP + diphosphate + H(+) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
CC         D-glutamate; Xref=Rhea:RHEA:58812, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:83900, ChEBI:CHEBI:142725, ChEBI:CHEBI:456215;
CC         EC=5.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_02209,
CC         ECO:0000269|PubMed:28294606};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58813;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02209,
CC         ECO:0000269|PubMed:28294606};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02209, ECO:0000305|PubMed:28294606}.
CC   -!- MISCELLANEOUS: The combined activity of MurD2 and MurL provides an
CC       alternative route for incorporating D-glutamate into peptidoglycan.
CC       {ECO:0000305|PubMed:28294606}.
CC   -!- SIMILARITY: Belongs to the MurL family. {ECO:0000255|HAMAP-
CC       Rule:MF_02209, ECO:0000305}.
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DR   EMBL; AP008229; BAE68074.1; -; Genomic_DNA.
DR   RefSeq; WP_011258235.1; NC_007705.1.
DR   AlphaFoldDB; P0DQD8; -.
DR   KEGG; xom:XOO1319; -.
DR   OMA; CRFVFLA; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02209; MurL; 1.
DR   InterPro; IPR043689; MurL.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Isomerase; Peptidoglycan synthesis.
FT   CHAIN           1..451
FT                   /note="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate
FT                   epimerase"
FT                   /id="PRO_0000446510"
SQ   SEQUENCE   451 AA;  49183 MW;  F130EB6F4BB978CD CRC64;
     MSAFDKHQIS TFRFVRCALD AQTGVATLVY AFDQGPELVE TVAVPGAPFA LGGANATAVQ
     QALQLLHLIA GVSYFKAAVP PNIAIDSYSI DAETAALVQS VYLHGLGEFA YRNGLQLHGK
     IRFPVAAQAA AAAPALGLRV HALVAIGGGK DSLVSIEALR HAGVDQTVSW IGGSQLIRAC
     AERTGLPVLN IGRVLAPELF ELNRQGAWNG HIPVTAVNSA ILVLAALLNG VDQVVFSNER
     SASYGSQIPG TGEVNHQWSK GWAFEQAFGD YVQRHVAADL RYYSLLRPLS ELAVARQFAK
     TDRYDAHFSS CNRNFHIMGE RPVHRWCGVC PKCHFVFLAL APFMPKTRLV NIFGRNLLDD
     ATQAGGYDAL LEFQDHKPFE CVGEGRESRT AMAVLASRAE WKEDAVVKRF IRDIQPQLDP
     NDLQVEPLMA IEGEHRIPPA LWERVRANFA V