ID A0A6G3DEK8_9ACTN Unreviewed; 506 AA. AC A0A6G3DEK8; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 02-OCT-2024, entry version 15. 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=GTY44_30170 {ECO:0000313|EMBL:MZG17694.1}; OS Streptomyces sp. SID5914. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=2690313 {ECO:0000313|EMBL:MZG17694.1, ECO:0000313|Proteomes:UP000477394}; RN [1] {ECO:0000313|EMBL:MZG17694.1, ECO:0000313|Proteomes:UP000477394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SID5914 {ECO:0000313|EMBL:MZG17694.1, RC ECO:0000313|Proteomes:UP000477394}; RX PubMed=30705269; DOI=.1038/s41467-019-08438-0; RA Chevrette M.G., Carlson C.M., Ortega H.E., Thomas C., Ananiev G.E., RA Barns K.J., Book A.J., Cagnazzo J., Carlos C., Flanigan W., Grubbs K.J., RA Horn H.A., Hoffmann F.M., Klassen J.L., Knack J.J., Lewin G.R., RA McDonald B.R., Muller L., Melo W.G.P., Pinto-Tomas A.A., Schmitz A., RA Wendt-Pienkowski E., Wildman S., Zhao M., Zhang F., Bugni T.S., Andes D.R., RA Pupo M.T., Currie C.R.; RT "The antimicrobial potential of Streptomyces from insect microbiomes."; RL Nat. Commun. 10:516-516(2019). 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|HAMAP-Rule:MF_00208, 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:MZG17694.1}. 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; WWHW01001089; MZG17694.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G3DEK8; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000477394; 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: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|HAMAP-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|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:MZG17694.1}; 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 34..109 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 123..323 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 346..477 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT MOTIF 419..422 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 42 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 125..131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 166..167 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 193 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 201 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 395 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 419..422 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 475 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 479 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 233 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 506 AA; 52795 MW; C35A0D60D1FD5A58 CRC64; MTYPGPPRPV RISATPLAEL ADQLGVTAPD GSAEITGITH DSRAVRPGDL YAALPGARLH GADFVTQAAG LGAAAVLTDP AGAERAAAAG LPALVVDDPR ARMGELAATI YGHPGRDLLQ IGITGTSGKT TTAYLVEGGL RTAKSTGLIG TVEMRIGDER IKSERTTPEA TDLQALFAVM RERGTEAVAM EVSSHALVLG RVDACFFDIA VFTNLSPEHM EFHSGMEDYF QAKAQLFTPA RSKLGVVNVD DEYGRRLANE ATVPVVTYSA EGHPDADWRA DEVEVGPLDS TFTVLGPKGE RIAAKSPLAG PFNVANTLAA IVALAAAGLD PQSAADGVAA VPGVPGRLER VDEGQPFFAV VDYAHKTDAV ESVLRALRKV TEGRLHVVLG CGGDRDTTKR EPMGAAVARF ADTAVLTSDN PRSEDPLAIL ATMLQGAASV PAHERGEVQV FEDRAAAITA AVARAEPGDT VLVAGKGHEQ GQDIAGVVRP FDDRQVLSEA IKKAQG //