ID MURE_PROM1 Reviewed; 509 AA. AC A2C0L8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 24-JAN-2024, entry version 101. 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}; OrderedLocusNames=NATL1_04641; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL1A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(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=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:0000255|HAMAP-Rule:MF_00208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-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; CP000553; ABM75028.1; -; Genomic_DNA. DR RefSeq; WP_011823215.1; NC_008819.1. DR AlphaFoldDB; A2C0L8; -. DR SMR; A2C0L8; -. DR KEGG; pme:NATL1_04641; -. DR eggNOG; COG0769; Bacteria. DR HOGENOM; CLU_022291_4_1_3; -. DR OMA; CFMEVSS; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002592; Chromosome. 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; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium; KW Nucleotide-binding; Peptidoglycan synthesis. FT CHAIN 1..509 FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6- FT diaminopimelate ligase" FT /id="PRO_1000012374" FT MOTIF 425..428 FT /note="Meso-diaminopimelate recognition motif" FT BINDING 32 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 117..123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 159..160 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 186 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 192 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 194 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 401 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 425..428 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 476 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT BINDING 480 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" FT MOD_RES 226 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208" SQ SEQUENCE 509 AA; 56281 MW; D98BD6E69F8DEDFB CRC64; MSRYLHTLLK AIDLQVRSGL ANPEIKNLST DSREIEKGDL FLGLDGEKVD GGTFWAKAIE RGACAAIISK KASLLNPPTN EDPVVILPEP VSLFMGKLAA DFWGKPSSEI CLIGITGTNG KTTTSFLIEF LTTSLGHPSA LFGTLINRWP NYEETSKYTT TFAVPLQAKL RKAVQAGVEY GAMEVSSHAL SQNRVAGCDF NGAIFTNLSR DHLDYHDSME SYFEAKASLF RSHLIDDDGP RSVINIDDKW GSILAKELNK KCWTCSLKEN SQIREKPDLY ISNLQIMQDG YMGKLHTPFG VGNFISPLIG EFNLMNMLQA IGILVQRGLP LNDLLEALNK FPGVPGRMQL INMDGFKVKD GYPLVIVDYA HTPDGLQNAL IASRSLTKKR LICVFGCGGD RDKGKRSKMG EVAAKFADYI VVTSDNPRQE DPIEIIKDIQ KGITIDSEIS VEPERSIAIQ FAIAKAKKND VVLIAGKGHE DYQILKDQTI YFDDREQARK ALSLRTDVI //