ID G2EE01_9FLAO Unreviewed; 450 AA.
AC G2EE01;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=BZARG_1818 {ECO:0000313|EMBL:EGV43425.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV43425.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV43425.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV43425.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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|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:EGV43425.1}.
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DR EMBL; AFXZ01000029; EGV43425.1; -; Genomic_DNA.
DR RefSeq; WP_008637414.1; NZ_AFXZ01000029.1.
DR AlphaFoldDB; G2EE01; -.
DR STRING; 1046627.BZARG_1818; -.
DR PATRIC; fig|1046627.3.peg.1745; -.
DR eggNOG; COG0773; Bacteria.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003730; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003730}.
FT DOMAIN 9..110
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 117..286
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 306..391
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 119..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ SEQUENCE 450 AA; 50009 MW; C5112C24E4EB68C9 CRC64;
MNLDSIKNVY FIGIGGIGMS ALARYFHANG KRVSGYDKTS SEITDALIDS GIPVHFEDSV
RYLEDYVLNN TNTLVVYTPA VPKSHKELVH FMHSGHRVLK RSEVLGVITA NTFCLAVAGT
HGKTTTTSIL GHIMKVCDVP VTAFLGGISE NYNSNLILNG TEVTVVEADE FDWSFLTLSP
NMACITSMDA DHLDIYGDAA ELEKSFNDFA HKLKEDGTLF VKNGLSIAGV TYGIEDDSDY
TAQNIKIENG TYIFDVKTPK ALIENIEFSL PGRHNLSNAL IALAMAVEYG CNHDQIVKAL
ASYTGVKRRF SYHIKRDDLV YIDDYAHHPE EINAVHQAVR EMYPGKEVLA IFQPHLFSRT
RDFVDDFAAS LSKFDEVMLL DIYPAREEPI EGVSSEWLLE KITNDNKLLI SKAELIDKVK
ASRAQVILTI GAGDIGEQVK HIKEALRHEN
//
