ID   MURC_SHEHH              Reviewed;         489 AA.
AC   B0TQN8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Shal_0456;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000931; ABZ75031.1; -; Genomic_DNA.
DR   RefSeq; WP_012275585.1; NC_010334.1.
DR   AlphaFoldDB; B0TQN8; -.
DR   SMR; B0TQN8; -.
DR   STRING; 458817.Shal_0456; -.
DR   EnsemblBacteria; ABZ75031; ABZ75031; Shal_0456.
DR   KEGG; shl:Shal_0456; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_6; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001317; Chromosome.
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.
FT   CHAIN           1..489
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000074754"
FT   BINDING         128..134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   489 AA;  53125 MW;  6109B1B11B2AAC5A CRC64;
     MSNKAEKYSQ LRSMIPEMRR VKHIYFVGIG GAGMGGIAEV LVNEGYKLSG SDIAESAVTQ
     RLAQLGATIY IGHDASQVKG MDVVVVSTAI SADNPELVAA KELRIPVVRR AEMLAELMRY
     RHGVAVAGTH GKTTTTSLIA SIYGEAERDP TFVIGGLLNS AGTNARLGHS RYLIAEADES
     DASFLHLQPM VSVVTNIEAD HMDTYEGDLE KLKTTFVDFL HNLPFYGVAV VCIDDPIVRE
     LIPRIGRRIV TYGFSDDADV QALDFKQTGY SCEFTVKRAG LADLRLSVNL PGEHNVLNAL
     AAIAVATEDD IEDAAIIKAL AEFQGIGRRF QQIGEFATSK GEIKLVDDYG HHPSEVAATI
     KAARLGWPER RLVMIYQPHR YSRTRDLYED FVEVLSQVDC LLMLDVYAAG EAPIPGADSR
     ALCRSIRVRG QVEPVFVAST EQLETILPEI LQGGDLLLTQ GAGSIGLLSR SLTESNLGFA
     ATGKDEKNA