ID   MURC_BART1              Reviewed;         475 AA.
AC   A9IWA4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BT_1590;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK01929.1; -; Genomic_DNA.
DR   RefSeq; WP_012232055.1; NC_010161.1.
DR   AlphaFoldDB; A9IWA4; -.
DR   SMR; A9IWA4; -.
DR   STRING; 382640.BT_1590; -.
DR   EnsemblBacteria; CAK01929; CAK01929; BT_1590.
DR   KEGG; btr:BT_1590; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_5; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001592; 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..475
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000336815"
FT   BINDING         114..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   475 AA;  52282 MW;  9E3663B2FDD329D1 CRC64;
     MKMPLDIGVI HFIGIGGIGM SGIAEVFYNL GYKVQGSDQV ESANVERLRR KGINVHIGHY
     AENLGNAEVV VFSTAVKKTN PEYIAAKERH LPLVRRAEML AELMRFRRAI AVGGTHGKTT
     TTSMVAALLD AGHFDPVVIN GGIINAYGTN SRTGEGDWMI VEADESDGTF LKLPADIAVV
     TNIDAEHLDH YGSFDAVRTA FRQFVENVPF YGFAVLCVDH PEVQSLAGRI DDRWVITYGA
     NPQADVRFLN LSRDGQKTHF DVLVRSRKTG RKIELKNLLL PMAGQHNVAN ATAAIAIAHE
     LGISNELIKK GLAEFGGVKR RFTRTGSWRG IEIFDDYGHH PVEIKAVLRA ARESAKGRVI
     AIAQPHRYSR LYHLFDDFAA CFNDADTVLI TPVYAAGEEP IVGFGSQELV EHIKMAGHRD
     VRLIHDLEDV VSLVSKFAQA EDYVVFLGAG NITQWACALP HRLSGLDGYD KFSAH