ID   MURC_VIBPA              Reviewed;         485 AA.
AC   Q87SG3;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=VP0461;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC         Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00046}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC58724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000031; BAC58724.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_796840.1; NC_004603.1.
DR   RefSeq; WP_005458174.1; NC_004603.1.
DR   AlphaFoldDB; Q87SG3; -.
DR   SMR; Q87SG3; -.
DR   STRING; 223926.28805444; -.
DR   EnsemblBacteria; BAC58724; BAC58724; BAC58724.
DR   GeneID; 1187929; -.
DR   KEGG; vpa:VP0461; -.
DR   PATRIC; fig|223926.6.peg.439; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_6; -.
DR   OMA; DITYQLR; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; 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   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00046; MurC; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01082; murC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..485
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182181"
FT   BINDING         129..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   485 AA;  52950 MW;  381BBE54E04A9041 CRC64;
     MTIQHTQDLA QIRAMVPEMR RVKCIHFIGI GGAGMSGIAE VLLNEGYEIT GSDLSENPVT
     ERLVSKGATV FIGHQASNVE KASVVVVSTA INEENPEVMA ARELRIPIVR RAEMLAELMR
     FRHGIAVAGT HGKTTTTALV TQIYSEAGLD PTFVNGGLVK SAGTNARLGS SRILIAEADE
     SDASFLHLQP MVSIVTNIEA DHMDTYGGDF ETLKQTFIDF LHNLPFYGQA IVCIDDPVIR
     ELIPRISRQV ITYGFSDDAD VRIENYHQEG QQGKFTVVRK GRANLDITLN IPGRHNALNA
     SAAIAVATED DIEDDAILKA MAGTQGTGRR FDHLGEFDTG NGHAMLVDDY GHHPTEVDVT
     IKAARSGWQD KRLVMIFQPH RYSRTRDLYD DFANVLEQVD VLIMLDVYAA GEKPIAGADG
     RSLCRTIRSR GKVDPIFVPE IEQLPSVLAN VIQDGDLILT QGAGDVGKVA KQLANLELNI
     NKMLG