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 28-FEB-2018, entry version 82. 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=NATL1_04641; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteria; Synechococcales; Prochloraceae; OC 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., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., 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 CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl- CC D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + CC UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6- CC diaminoheptanedioate. {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: Carbamoylation 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 ProteinModelPortal; A2C0L8; -. DR SMR; A2C0L8; -. DR STRING; 167555.NATL1_04641; -. DR EnsemblBacteria; ABM75028; ABM75028; NATL1_04641. DR KEGG; pme:NATL1_04641; -. DR eggNOG; ENOG4107EEN; Bacteria. DR eggNOG; COG0769; LUCA. DR HOGENOM; HOG000268118; -. DR KO; K01928; -. DR OMA; CFMEVSS; -. DR OrthoDB; POG091H0082; -. DR BioCyc; PMAR167555:G1G7Z-449-MONOMER; -. 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-KW. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC. 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-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Nucleotide-binding; Peptidoglycan synthesis. FT CHAIN 1 509 UDP-N-acetylmuramoyl-L-alanyl-D- FT glutamate--2,6-diaminopimelate ligase. FT /FTId=PRO_1000012374. FT NP_BIND 117 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 159 160 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 425 428 Meso-diaminopimelate binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT MOTIF 425 428 Meso-diaminopimelate recognition motif. FT BINDING 32 32 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 186 186 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 192 192 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 194 194 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 401 401 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 476 476 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 480 480 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT MOD_RES 226 226 N6-carboxylysine. {ECO:0000255|HAMAP- FT 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 //