ID C1A0Y0_RHOE4 Unreviewed; 544 AA. AC C1A0Y0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 20-APR-2010, entry version 9. DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; DE EC=6.3.2.13; GN Name=murE; OrderedLocusNames=RER_35570; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=234621; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the murCDEF family. 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; YP_002767004.1; -. DR GeneID; 7712246; -. DR GenomeReviews; AP008957_GR; RER_35570. DR KEGG; rer:RER_35570; -. DR OMA; EHLDFHG; -. DR ProtClustDB; PRK00139; -. 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-...; IEA:EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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 Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1. DR Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; Mur_ligase_C; 1. DR SUPFAM; SSF53623; Mur_ligase_cen; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW Auxin biosynthesis; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Ligase; KW Nucleotide-binding; Peptidoglycan synthesis. 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 //