ID   MURL_SALTO              Reviewed;         457 AA.
AC   A4X982;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=Strop_3006 {ECO:0000312|EMBL:ABP55443.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02209, 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; CP000667; ABP55443.1; -; Genomic_DNA.
DR   RefSeq; WP_012014221.1; NC_009380.1.
DR   AlphaFoldDB; A4X982; -.
DR   STRING; 369723.Strop_3006; -.
DR   EnsemblBacteria; ABP55443; ABP55443; Strop_3006.
DR   KEGG; stp:Strop_3006; -.
DR   PATRIC; fig|369723.5.peg.3093; -.
DR   eggNOG; COG1365; Bacteria.
DR   HOGENOM; CLU_045660_0_0_11; -.
DR   OMA; CRFVFLA; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000235; Chromosome.
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; Reference proteome.
FT   CHAIN           1..457
FT                   /note="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate
FT                   epimerase"
FT                   /id="PRO_0000446512"
SQ   SEQUENCE   457 AA;  49014 MW;  F4B6ADE85C0E8D34 CRC64;
     MPNEQLRRMD AFTFPSYSFD LSTGEALFDY ALTGPDGEQR FTEVITLPLP ASPPSDERVA
     TLGRVLELLH VIAGVSYYKT AAPHRLVLPA PLGPSAVALV TAVYTKGLAE YAYRNALPHV
     LRLRPEVPSG EVTPPVGYDT DGRRPLSAVG GGKDSIVSLE ALRRDGLDPL PFSVNPNRVI
     EAVNVASGLP ALAARRRIDP VLFDLNAAGA LNGHIPVTAI NSLIAVATSV LNGLGPVVMS
     NERSASDPNL IWDGHQINHQ WSKGVEAEGL LRGALEEHAG LTDPYFSLLR QLSELHIART
     FARIGGYDDV VTSCNAAFKL RGASDRWCRD CPKCRFVFLA LAPFMPRERI TRVFGGDLLA
     DPAQLPGYRE LLGVDGHKPF ECVGEVEESV VALSLLGEQS GWRDAPVVSA LIDAVPETAW
     KTAATSAVFT PGGPSFTPTR YADALGSLTE PARNLPG