ID MURE_GEOTN Reviewed; 489 AA. AC A4IM04; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 104. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; GN OrderedLocusNames=GTNG_0980; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus. OX NCBI_TaxID=420246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2; RX PubMed=17372208; DOI=10.1073/pnas.0609650104; RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., RA Han W., Peng X., Liu R., Wang L.; RT "Genome and proteome of long-chain alkane degrading Geobacillus RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007). 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:0000255|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- CC diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma- CC D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+); CC Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, CC ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00208}. 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; CP000557; ABO66358.1; -; Genomic_DNA. DR RefSeq; WP_011887098.1; NC_009328.1. DR AlphaFoldDB; A4IM04; -. DR SMR; A4IM04; -. DR KEGG; gtn:GTNG_0980; -. DR eggNOG; COG0769; Bacteria. DR HOGENOM; CLU_022291_4_1_9; -. DR UniPathway; UPA00219; -. 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:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro. DR FunFam; 3.40.1390.10:FF:000005; UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase; 1. DR FunFam; 3.90.190.20:FF:000006; UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase; 1. 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 NCBIfam; NF001124; PRK00139.1-2; 1. DR NCBIfam; NF001126; PRK00139.1-4; 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; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium; KW Nucleotide-binding; Peptidoglycan synthesis. FT CHAIN 1..489 FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6- FT diaminopimelate ligase" FT /id="PRO_1000012355" FT MOTIF 407..410 FT /note="Meso-diaminopimelate recognition motif" 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:0000255|HAMAP-Rule:MF_00208" FT BINDING 108..114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 149 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 150..151 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 177 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 183 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 185 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 383 FT /ligand="meso-2,6-diaminopimelate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 407..410 FT /ligand="meso-2,6-diaminopimelate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 459 FT /ligand="meso-2,6-diaminopimelate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 463 FT /ligand="meso-2,6-diaminopimelate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT MOD_RES 217 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" SQ SEQUENCE 489 AA; 53536 MW; 59FF7596C049AEEF CRC64; MKLQTLLSRL PGFWVHRGGN PDIVALEMDS RHVTPGSLFF CVKGFTVDGH DFAEQAVERG AVAIVAERPL SVNVPVVVVP DSRRAMAILA DAFYGQPTHR LHLIGVTGTN GKTTTTHIIE QVARKAGKKI GLIGTVGTKI GDRSYPAVNT TPESLVLQRT FKQMVDEGVE FVTMEVSSHA LHQGRVHGCD YDVAVFTNLT QDHLDYHGTM EEYRNAKGLL FAQLGNRYDE RRPKFAVLNH DDPVSQYYKH MTAAPIITYG IKEKSDVMAE QIEMTPGGMA FQLCTPHGTM AIETKLVGLF NVYNLLAATA ACLASGFSLA TIAEALANVS PVPGRFETVD EGQNFTVIVD YAHTPDSVEN ALKTVRQFAK RNVYVVIGCG GDRDRTKRPL MAQAAVRYAD VAVFTSDNPR SEDPRQILRD MEAGVSAGDG TYVTIPDREE AIRYAIGQAQ EGDVVLIAGK GHETYQIIGD DVIDFDDRAV ARAAVKERR //