ID J3B2Y4_9PSED Unreviewed; 487 AA. AC J3B2Y4; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 28-FEB-2018, entry version 37. 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=PMI31_01108 {ECO:0000313|EMBL:EJM76848.1}; OS Pseudomonas sp. GM55. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144333 {ECO:0000313|EMBL:EJM76848.1, ECO:0000313|Proteomes:UP000007268}; RN [1] {ECO:0000313|EMBL:EJM76848.1, ECO:0000313|Proteomes:UP000007268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM55 {ECO:0000313|EMBL:EJM76848.1, RC ECO:0000313|Proteomes:UP000007268}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). 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: 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: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|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135, CC 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:EJM76848.1}. 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; AKJJ01000032; EJM76848.1; -; Genomic_DNA. DR RefSeq; WP_008016696.1; NZ_AKJJ01000032.1. DR EnsemblBacteria; EJM76848; EJM76848; PMI31_01108. DR PATRIC; fig|1144333.3.peg.1043; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000007268; 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: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; 3.40.1190.10; -; 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|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951553}; KW Cell division {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951537}; KW Cell shape {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951545}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951523}; KW Complete proteome {ECO:0000313|Proteomes:UP000007268}; 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}; 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|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951548}. FT DOMAIN 19 94 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 106 306 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 329 410 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 108 114 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 150 151 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 402 405 Meso-diaminopimelate binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT MOTIF 402 405 Meso-diaminopimelate recognition motif. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 23 23 UDP-MurNAc-L-Ala-D-Glu; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 25 25 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 177 177 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 183 183 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 185 185 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 378 378 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT BINDING 453 453 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 457 457 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT MOD_RES 217 217 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 487 AA; 52115 MW; 0DE81793E58C6663 CRC64; MSLSLNKIFP HAGHDLLIRE LALDSRKVRA GDLFLAVPGG KFDGRAHIAD ALQRGAAAVA YEVEGATVLP ITEVPLIPVK GLAAQLSDIA GRFYGEPSHH LNLVGVTGTN GKTSVTQLVA QALDLLGQHC GLVGTLGCGF YGSLESGLHT TPNPIAMQAT LADLKKAGAK AVAMEVSSHG LDQGRVTALA FDVAVMTNLS RDHLDYHGTM QAYGETKAKL FAWNDLKCRV VNLDDEFGRQ LAADEGESRL ITYSLEDSRA YLYCREAQFN DEGVRATLVT PQGEHLLRSA LLGRFNLSNV LAAVGALLGL DYALDEILKV LPMLEGPAGR MQRLGGGSQP LVVVDYAHTP DALEKVLLAL RPHAKGRLLC LFGCGGDRDR GKRPLMAEVV ERLADGVLVT DDNPRTEDPS VIFDDIRAGF TAVDKVEFVA GRGQAIARLI ASASVDDVIV LAGKGHEDYQ EINGERHAFS DLVEADHALT AWEVAHV //