ID A0A2J9DYJ0_9GAMM Unreviewed; 583 AA. AC A0A2J9DYJ0; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 16-JAN-2019, entry version 6. 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=A6J60_006780 {ECO:0000313|EMBL:PNK60605.1}; OS Psychrobacter sp. FDAARGOS_221. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK60605.1, ECO:0000313|Proteomes:UP000217719}; RN [1] {ECO:0000313|EMBL:PNK60605.1, ECO:0000313|Proteomes:UP000217719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_221 {ECO:0000313|EMBL:PNK60605.1, RC ECO:0000313|Proteomes:UP000217719}; RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Sengamalay N., RA Ott S., Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., RA Geyer C., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. 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: CC Reaction=ATP + meso-2,6-diaminopimelate + 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- CC diaminopimelate; 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; Evidence={ECO:0000256|HAMAP- CC 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: 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:PNK60605.1}. 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; NWFK02000001; PNK60605.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000217719; 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; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. 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 TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Complete proteome {ECO:0000313|Proteomes:UP000217719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:PNK60605.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}. FT DOMAIN 178 399 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 423 506 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 180 186 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 226 227 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 498 501 Meso-diaminopimelate binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT MOTIF 498 501 Meso-diaminopimelate recognition motif. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 73 73 UDP-MurNAc-L-Ala-D-Glu; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 75 75 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 253 253 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 259 259 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 261 261 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 474 474 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT BINDING 551 551 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 555 555 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT MOD_RES 293 293 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 583 AA; 62874 MW; 3DEEA30B97D06C4F CRC64; MTTHTSHSDT PSNNTAQENT TVSALTLQQL LTTAQQVLPH HKNTLQHMLQ DAEQAVSTEQ GALLQLPVSQ FVLDSRQLTT DAATKDIFVL LKSHTQPIEK SQQYAQAAAQ QAACIISEID PADLQLSEQD IGCPLLYVPN IRDVLGTLIQ LSLLPSSTLS QIQSTQDLLQ QLPQVIAVTG TNGKTTISQL IAQLCHLSAL PELADSAVMG TAGNGRLGSL VQASHTTGDA LAVQRFLRQM QQEGVDVLAL EASSHGLDQQ RLQGVPVKVA VYSNLSRDHL DYHPDMQDYA RAKARLFDKA YFPQLTHAII NIDDDFAPMM AKTAIDSGVK VWLYSLNPEV SVNIDGVDAL FVASSISPSL TGVEIELTVD SNSIATDSIK LHSPLLGRFN VANVLAAVAG AMALGVPLDA MPALVKQLQG ASGRMQRAES ANDDQGVFIV DYAHTPDALT QVLTSLKSHC EGKLWAVFGC GGDRDKGKRP LMAQAGLSVA DQVVLTSDNP RSEDPVLILE DMQQGMTEAQ HQKTTVIADR KQAINYVVQQ AGAQDIVVIA GKGHETYQEI KGVRYDFDDR LILQEALIEA HQG //