ID A0A417RJD3_9CLOT Unreviewed; 499 AA. AC A0A417RJD3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-MAY-2024, entry version 25. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208}; GN ORFNames=DXB77_03215 {ECO:0000313|EMBL:RHV12642.1}; OS Clostridium sp. OM05-9. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=2293045 {ECO:0000313|EMBL:RHV12642.1, ECO:0000313|Proteomes:UP000285915}; RN [1] {ECO:0000313|EMBL:RHV12642.1, ECO:0000313|Proteomes:UP000285915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OM05-9 {ECO:0000313|EMBL:RHV12642.1, RC ECO:0000313|Proteomes:UP000285915}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) CC in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; CC EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135}. CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}. 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:RHV12642.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QULF01000002; RHV12642.1; -; Genomic_DNA. DR AlphaFoldDB; A0A417RJD3; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000285915; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1. DR HAMAP; MF_00208; MurE; 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; IPR035911; MurE/MurF_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR NCBIfam; TIGR01085; murE; 1. DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1. DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00208}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:RHV12642.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00208}. FT DOMAIN 23..96 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 108..310 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 329..415 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT MOTIF 404..407 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 30 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 110..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 151 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 152..153 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 179 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 187 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 380 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 404..407 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 456 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 460 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 221 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 499 AA; 55336 MW; BB208B01FE14C037 CRC64; MKASELLKGL QYSVICGDED IEIKEIYNDS RKVGAQGLFF CIVGAKFDGH EYIKDVTEKG AVCLIVQKDV NPVPGVLIVK VESTRYAMGI VSSNFYGNPS SKLTVIGITG TKGKTTTTYM IREMLMSAGH KTGLIGTIEI MDGKEVIPAN NTTPESMIVH KKLKDMLDNG LDSVVMEVSS QGLMLDRVAG VDFDYGIFSN LSRDHIGPNE HKTFEEYAMW KSKLFTMCKT GIFNADDAHV DTMTEHAACK IVTYGIHGDY DYKANDHNLY NKDGHLGIGY HLSGKLNGDV LVNLPGNFSI YNSLAAIAVA DLMGVSFDKI QAILKTIKVK GRVELIPISD KFTIMIDYAH NAVSLESILE TLREYNPGRL VSLFGCGGDR SKERRFEMGE VSGNMADLTI ITSDNPRSED PQAIINDIKT GIDKTTGKYV EIIDRKEAIR YAIMHAEPGD VIVLAGKGHE DYQEIKGVKY HMDERDLIRE ILEEEDVTKI CGYNNRYFA //