ID A0A417RJD3_9CLOT Unreviewed; 499 AA. AC A0A417RJD3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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; Firmicutes; Clostridia; Clostridiales; 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 RT microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminopimelate + 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- CC diaminopimelate; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135, CC ECO:0000256|SAAS:SAAS00951514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}. CC -!- PTM: Carbamoylation 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|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00219; -. DR Proteomes; UP000285915; Unassembled WGS sequence. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 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 Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951530}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523}; KW Complete proteome {ECO:0000313|Proteomes:UP000285915}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951519}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:RHV12642.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951542}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}; KW Reference proteome {ECO:0000313|Proteomes:UP000285915}. FT DOMAIN 23 96 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 108 310 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 329 415 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 110 116 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 152 153 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 404 407 Meso-diaminopimelate binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT MOTIF 404 407 Meso-diaminopimelate recognition motif. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 151 151 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 179 179 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 187 187 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 380 380 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT BINDING 456 456 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 460 460 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT MOD_RES 221 221 N6-carboxylysine. {ECO:0000256|HAMAP- FT 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 //