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Database: UniProt
Entry: A0A2A7MBW7_9CLOT
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ID   A0A2A7MBW7_9CLOT        Unreviewed;       458 AA.
AC   A0A2A7MBW7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000256|HAMAP-Rule:MF_00639};
GN   ORFNames=CQ394_19895 {ECO:0000313|EMBL:PEG28923.1};
OS   Clostridium neonatale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG28923.1, ECO:0000313|Proteomes:UP000220840};
RN   [1] {ECO:0000313|EMBL:PEG28923.1, ECO:0000313|Proteomes:UP000220840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG28923.1,
RC   ECO:0000313|Proteomes:UP000220840};
RA   Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT   "Effective Description of Clostridium neonatale sp. nov. linked to
RT   necrotizing enterocolitis in neonates and a clarification of species
RT   assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT   Rainey 2016.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00639};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00639}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639}.
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:PEG28923.1}.
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DR   EMBL; PDCJ01000006; PEG28923.1; -; Genomic_DNA.
DR   RefSeq; WP_058293108.1; NZ_PDCJ01000006.1.
DR   AlphaFoldDB; A0A2A7MBW7; -.
DR   STRING; 137838.GCA_001458595_00087; -.
DR   OrthoDB; 9809796at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000220840; 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:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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_00639; MurD; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   NCBIfam; TIGR01087; murD; 1.
DR   PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF21799; MurD-like_N; 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_00639}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00639};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00639}; Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220840}.
FT   DOMAIN          122..294
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   458 AA;  51326 MW;  799B0B692AF12DF5 CRC64;
     MKRDFKEFKD FICGKNVGVV GIGVSNIPLI NFLLDLGAKV TAFDKKNKED LGNVADEFSK
     KGVTLELGEH YLDNLTGFDV IFKTPSMRID SEALVRAKNE GAYVTSEMEE FVKYTKGKIY
     AITGSDGKTT TTTIVSKLLE EEGYKTWVGG NIGTPLFAQI ENIKDDDKVV LELSSFQLMT
     MHEKINVAIC TNLAPNHLDM HKDMQEYIDS KKNIFLYQND DDVLVVNREN DITYSFEKEA
     KGKVREFSSK RVIKDGAYLK DNILYLEGKE VCDRDDIIIK GVHNVENYLA AFIATKDDVS
     IETMKKIAQT FAGVEHRCEL VREIDGVKYY NDSIASSPTR TLAGVKAFNE KVILIAGGYD
     KNIPFEPLAY EGYPYIKTLI LLGKTKDKIK LVFDKLEKEK GIKVDIKTVS SLDEAVDVAK
     KIARSGDIVT LSPACASFDM FPNFMARGNV FKEIVNSL
//
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