ID C1A0Y0_RHOE4 Unreviewed; 544 AA. AC C1A0Y0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 13-NOV-2019, entry version 77. 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 ECO:0000313|EMBL:BAH34265.1}; GN OrderedLocusNames=RER_35570 {ECO:0000313|EMBL:BAH34265.1}; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH34265.1, ECO:0000313|Proteomes:UP000002204}; RN [1] {ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus RT erythropolis PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAH34265.1, ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x; RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N., RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K., RA Ito M., Narita H., Tago S., Fujita N., Harayama S.; RT "Sequence analysis of three plasmids harboured in Rhodococcus RT erythropolis strain PR4."; RL Environ. Microbiol. 8:334-346(2006). 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 ECO:0000256|SAAS:SAAS00951514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}. CC -!- PTM: Carboxylation 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 --------------------------------------------------------------------------- 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; AP008957; BAH34265.1; -; Genomic_DNA. DR RefSeq; WP_020908075.1; NC_012490.1. DR STRING; 234621.RER_35570; -. DR EnsemblBacteria; BAH34265; BAH34265; RER_35570. DR KEGG; rer:RER_35570; -. DR PATRIC; fig|234621.6.peg.4073; -. DR eggNOG; ENOG4107EEN; Bacteria. DR eggNOG; COG0769; LUCA. DR HOGENOM; HOG000268118; -. DR KO; K01928; -. DR OMA; CFMEVSS; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002204; 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; 3.40.1190.10; -; 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|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523}; KW Complete proteome {ECO:0000313|Proteomes:UP000002204}; 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, ECO:0000313|EMBL:BAH34265.1}; 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|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}. FT DOMAIN 52 132 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 146 354 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 374 458 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 148 154 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 1 20 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 190 191 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 449 452 Meso-diaminopimelate binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT MOTIF 449 452 Meso-diaminopimelate recognition motif. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 57 57 UDP-MurNAc-L-Ala-D-Glu; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 217 217 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 225 225 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 425 425 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT BINDING 505 505 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 509 509 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT MOD_RES 257 257 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 544 AA; 57195 MW; 02C57687F164A449 CRC64; MPNRLQSSNS DGAPGTRPTQ PVATAITALS ELSGARLEWV GQPGSQSSEV VVKGVDLRAQ GIVADDLFAA LPGARTHGAQ FAVDALGRGA TAILTDEAGL ELIEAAGKAP DRSVPVLVHP NPRDVLGEIS AEIYGRPSEK MQVVGITGTS GKTTTSYLLE AAIAGAGRKP GLVGTIETRI DGRRVPSALT TPEAPQLHAL FAVMAEQGID TVVMEVSSHA LALGRVDGIR FDIGAFTNLS QDHLDFHRDF EEYFQAKARL FDPESTVRAE HAVVCVDDVW GRRMAELAAT DESDAVTTVS TSTAEAEWKV GAVEVAEDGS QTFELVGPDG QSWPVSLRLP GRYNVANAAL ALTVSFAAGL DPDAAVRALG TVDVPGRVQR IDRGQSFLAV VDYAHKPAAL EAVIATLRNQ VPGRVAVVVG AGGDRDAGKR TLMGEAGARG ADLLIVTDDN PRTEDPAKIR ASVMQGAIDV PESERGEIRE VGDRALAIEQ AVRWAQPGDV VLVAGKGHEV GQEIDGVKHP FDDREVLGEM IGRFAINTAH GGKQ //