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Database: UniProt
Entry: I4M2C6_GARVA
LinkDB: I4M2C6_GARVA
Original site: I4M2C6_GARVA 
ID   I4M2C6_GARVA            Unreviewed;       525 AA.
AC   I4M2C6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000256|HAMAP-Rule:MF_00046};
GN   ORFNames=CGSMWGv1500E_02222 {ECO:0000313|EMBL:EIK83366.1};
OS   Gardnerella vaginalis 1500E.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=698957 {ECO:0000313|EMBL:EIK83366.1, ECO:0000313|Proteomes:UP000032875};
RN   [1] {ECO:0000313|EMBL:EIK83366.1, ECO:0000313|Proteomes:UP000032875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1500E {ECO:0000313|EMBL:EIK83366.1,
RC   ECO:0000313|Proteomes:UP000032875};
RX   PubMed=22609915; DOI=10.1128/JB.00056-12;
RA   Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA   Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA   Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT   "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT   vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT   Consistent with Subspeciation into Genovars.";
RL   J. Bacteriol. 194:3922-3937(2012).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP-
CC         Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIK83366.1}.
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DR   EMBL; ADES01000007; EIK83366.1; -; Genomic_DNA.
DR   RefSeq; WP_004127584.1; NZ_ADES01000007.1.
DR   AlphaFoldDB; I4M2C6; -.
DR   PATRIC; fig|698957.3.peg.436; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000032875; Unassembled WGS sequence.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01082; murC; 1.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00046};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00046}.
FT   DOMAIN          36..133
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          138..356
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          377..460
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         140..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   525 AA;  55644 MW;  AD5A44724DCE72C7 CRC64;
     MSNVNNNADL LCSKITLNPI KAAFEDSKNA STLGRVHFIG IGGAGMSVLA EMLHEEGVSV
     SGCDREENDH TKRLEELGIS VEIGQNASHV ESADVLVYSS AIKPNNPEIV AAYANGVKLV
     HRSDILALLL ASKTGVTVAG AHGKTTTSSL LSHILSVAGT GELSDPSYAI GGSIQAADGT
     VIDGGHAGKG SVMVAEADES DGSFEKYRPS IAIVTNAEAD HLDHYGSSER YREAFVEHVS
     HAIDHVIICA DDEGARKVLE KMSDETLRAT IAYGAYDSWA STSARVQNLA QFAGIKHESE
     QAVSGREVFT LVLPGNIAGN IAGNAGKIED SVSLEVSLLI PGLHNARNAS AAIIAAVLLG
     MKPEDAARGA QSFRGASRRF DIRGCVNGVT VVDDYAHHPT EIEALLRAAR RRYTSAKLRV
     LFQPHLFSRT RAFASEFANA LALADDVIVT GIFPAREKQE DFPNIHAETI VEAAKSQNLN
     VQIEAVENMR EAALKLAARA KFGDVLLTVG AGSITDMTSV MLEAL
//
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