ID   MURC_AERHH              Reviewed;         484 AA.
AC   A0KPX1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=AHA_3883;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37350.1; -; Genomic_DNA.
DR   RefSeq; WP_010635950.1; NC_008570.1.
DR   RefSeq; YP_858322.1; NC_008570.1.
DR   AlphaFoldDB; A0KPX1; -.
DR   SMR; A0KPX1; -.
DR   STRING; 380703.AHA_3883; -.
DR   EnsemblBacteria; ABK37350; ABK37350; AHA_3883.
DR   GeneID; 58196597; -.
DR   GeneID; 64360411; -.
DR   KEGG; aha:AHA_3883; -.
DR   PATRIC; fig|380703.7.peg.3853; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_6; -.
DR   OMA; DITYQLR; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:A0KPX1; -.
DR   Proteomes; UP000000756; 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..484
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000071092"
FT   BINDING         126..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   484 AA;  52326 MW;  48B588E3A253ECC0 CRC64;
     MTKVELAKLR TVIPEMRRVR RIHFIGIGGA GMGGIAEVLA NEGYQVTGSD LARNAVTERL
     ESLGAHIFVG HSAEHVNEAS VVVVSTAIKQ DNPELLAARE LRIPVVRRAE MLAELMRFRH
     GIAIAGTHGK TTTTSLVASI YAEADRDPTF VIGGLLNSAG TNARLGSSRY LIAEADESDA
     SFLHLQPMVS IVTNIEADHM DTYGGDFSKL KATFIDFLHN LPFYGLAVVC VDDPVIRGML
     PEIARPTITY GLSDDADVQV LDFVQTSNRS RFRVRRKDAG ELEVTLNLPG IHNALNAAAA
     IAVATEDGIG DDAIIRALAK FEGVGRRFQQ YGEFETGRGK AMLVDDYGHH PSEVKVTINA
     ARAGWPEKRL VMVFQPHRYT RTRDLYEDFA DVLSKVDVLV MLEVYAAGEE PIPGADGRAL
     CRSIRSRGSL EPIFVATPDD VPAVLAGLVG EGDLVLTQGA GNVGALARRL GEMKLSIESM
     KSGA