ID   MURC_ACISJ              Reviewed;         477 AA.
AC   A1WC05;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Ajs_3669;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) 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; CP000539; ABM43780.1; -; Genomic_DNA.
DR   RefSeq; WP_011806763.1; NC_008782.1.
DR   AlphaFoldDB; A1WC05; -.
DR   SMR; A1WC05; -.
DR   STRING; 232721.Ajs_3669; -.
DR   EnsemblBacteria; ABM43780; ABM43780; Ajs_3669.
DR   KEGG; ajs:Ajs_3669; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_4; -.
DR   OMA; DITYQLR; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000645; 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; Reference proteome.
FT   CHAIN           1..477
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000004304"
FT   BINDING         112..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   477 AA;  50331 MW;  26D8A90DA179FCDD CRC64;
     MKQAIRHIHF VGIGGSGMCG IAEVLHNLGY VVSGSDLADS PTLRRLQSLG VATHVGHAAA
     HIAGADAVVT STAVQADNPE VLAARERKIP VVPRALMLTE LMRLRKGIAI AGAHGKTTTT
     SLVASVLGEA GLDPTFVIGG RLNSAGTNAK LGQGEYIVVE ADESDGSFLN LLPVMAVVTN
     IDADHMETYG HDFGRLKQAF VDFLHRMPFY GTAILCIDNP AVRDILPLVT CPVTSYGLSE
     DAEVRAVDVR AVGTQMHFTV QRRNGVTLPD LQVVLNLAGE HNVLNALAVI AVAAELNVPD
     DALLRALAGF TGVGRRFQRH GDLPAQGGGH FTLIEDYGHH PVEMAATLAA ARGAYPGRRL
     VLAFQPHRYS RTRDCFEDFV KVLGTADAVL LTEVYAAGEA PIVAADGRSL ARALRVAGTV
     EPVFIDNVAD MPQRIAAGAR DGDVVLCMGA GSIGGVPAKV VDLLQKNELL AQEGRAQ