ID   MURC_BIFLO              Reviewed;         512 AA.
AC   Q8G4Q4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=BL1324;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25124.1; -; Genomic_DNA.
DR   RefSeq; NP_696488.1; NC_004307.2.
DR   RefSeq; WP_007054402.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4Q4; -.
DR   SMR; Q8G4Q4; -.
DR   STRING; 206672.BL1324; -.
DR   EnsemblBacteria; AAN25124; AAN25124; BL1324.
DR   KEGG; blo:BL1324; -.
DR   PATRIC; fig|206672.9.peg.175; -.
DR   HOGENOM; CLU_028104_2_1_11; -.
DR   OMA; HLEHYNN; -.
DR   PhylomeDB; Q8G4Q4; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000439; 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..512
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182059"
FT   BINDING         132..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   512 AA;  53398 MW;  D41AC19B2CA2C15D CRC64;
     MSQDQPIVLD PTYASFDAAA RPADLGATHF IGIGGAGMSV LAEMLHAEGV AVDGSDRAHS
     AKTDRLETLG ITVEFGQRAE NVAQAETVVY SSAIKPDNPE IVAAHAAGKR IVHRSDILAL
     LMNGKRAVTV AGAHGKTTTS SMLSHILVNA GADPSYAIGG FIQGPDGTTL DGGHAGKGDI
     LVAEADESDG SFAKYHPTIA IITNCEADHL DHYGDEAHYR AAFVAHAGRA TGHVIISIDD
     PDGLAVLEAL PADVKSHTVA YGTTARESLP DLGGAAYVWI ASESETAGSG VEQLTLHLPA
     AVTAGEPVSQ SVALKVPGVH NARNAAAAIS AAVLLGVSPA DAAKAAGTFL GAARRFQVRG
     TVKQVTVVDD YAHHPTEIAA LLDAARRRYP DSTIRVIFQP HLFSRTKFFA HQFAKSLAKA
     DDVIITGIFP AREKQADFPD ISPSTIVDAA AGLKDASAGT WIQPVEDMCL AAKMMAMRAH
     HGDVIFTVGA GDITDMDQVL LTALEAHRES CE