ID C1A0Y0_RHOE4 Unreviewed; 544 AA. AC C1A0Y0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 17-FEB-2016, entry version 55. DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|SAAS:SAAS00085409}; DE EC=6.3.2.- {ECO:0000256|SAAS:SAAS00276926}; GN Name=murE {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}; 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085391}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135, CC ECO:0000256|SAAS:SAAS00085486}. 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 GeneID; 7712246; -. DR KEGG; rer:RER_35570; -. DR PATRIC; 23193590; VBIRhoEry66701_4073. DR eggNOG; COG0769; LUCA. DR eggNOG; ENOG4107EEN; Bacteria. DR HOGENOM; HOG000268118; -. DR KO; K01928; -. DR OMA; VDYAHTG; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; RERY234621:GHDE-3598-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002204; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00208; MurE; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_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|SAAS:SAAS00459289}; KW Cell cycle {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459322}; KW Cell division {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459379}; KW Cell shape {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459388}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459257}; KW Complete proteome {ECO:0000313|Proteomes:UP000002204}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00459408}; KW Ligase {ECO:0000256|SAAS:SAAS00459363, ECO:0000313|EMBL:BAH34265.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00459299}; KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459442}; KW Reference proteome {ECO:0000313|Proteomes:UP000002204}. 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}. 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 //