ID A0A1I5UH57_9BACT Unreviewed; 456 AA.
AC A0A1I5UH57;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN04515674_107180 {ECO:0000313|EMBL:SFP94560.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFP94560.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFP94560.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOXH01000007; SFP94560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5UH57; -.
DR STRING; 1079859.SAMN04515674_107180; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199306; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000199306};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..111
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 118..295
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 315..399
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 120..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ SEQUENCE 456 AA; 50847 MW; 01AD9295AE5AC5FC CRC64;
MNLKELKYIY FLGIGGIGMS AIARWFIANG YQLAGYDKTA TPLTDALKAE GIPVHFEDDI
SLIPEAFLQN PAQTLVVYTP AIPKNHREYN FLIDNGFTLM KRSQVLGLLT RNMFTVAVAG
THGKTTTSSM VAHILKNGGK NVTAFLGGIT QNYGTNFLLN EGMNEIMCVV EADEFDRSFL
TLFPDLAIVT STDADHLDIY GDHDHVLKSF QMFVGQIKPG GKLYQREGLH LQAYTNNETK
EFSLNNGDFH AENLRIENAE MIFDIVYPDG KITDVSMLIP GFHNVENALA ATAVALQAGV
SPEKVKEGIC TFKGVKRRFE YHVRNKDVVY IDDYAHHPTE IQAFLSSVKA LYPNRKLTAI
FQPHLFSRTN DFQDGFAESL DLADDLLLLD IYPARELPME GVTSQIIFDK MKLKDKVICS
KEEVLNLLTQ KKPELVVTIG AGDIDTLIPK IKGLLN
//
