ID A0A0B7J4R2_PHOPO Unreviewed; 511 AA. AC A0A0B7J4R2; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 29-APR-2015, entry version 2. DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|SAAS:SAAS00085409}; GN Name=murE {ECO:0000313|EMBL:CEO38066.1}; GN ORFNames=PPBDW_I20078 {ECO:0000313|EMBL:CEO38066.1}; OS Photobacterium phosphoreum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=659 {ECO:0000313|EMBL:CEO38066.1}; RN [1] {ECO:0000313|EMBL:CEO38066.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANT-220 {ECO:0000313|EMBL:CEO38066.1}; RA Genoscope - CEA; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:CEO38066.1}. 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; CCAR020000004; CEO38066.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC. 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:SAAS00085443}; KW Cell cycle {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00085467}; KW Cell division {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00085386}; KW Cell shape {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00085370}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00085405}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00085419}; KW Ligase {ECO:0000256|SAAS:SAAS00085462, ECO:0000313|EMBL:CEO38066.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00085432}; KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00085400}. SQ SEQUENCE 511 AA; 54343 MW; 57C93013B58225D4 CRC64; MSVIMALVKQ EVQLGALLAP WLTAKNVPAE YAQLLLTTMT LDSRQVTAGC LFAAVNGHTV DGRRFIANAI AAGASAIVAE AEGVASDGEI QFQDGIIIIY LHHLGHKLSA IAGRFYAEPD SKLKLYAVTG TNGKTTISQL LAQWADLIGY RAGVMGTTGN GLLTDLQPAA NTTGSAIEVQ QTLAELVTQG ANFAAMEVSS HGLVQGRVSA LHFVASIFTN LSRDHLDYHG DMAHYAAAKK SLFTEHDSGV AVINADDAIG QQWLADLPQA VAVAMNAEAV VAHSGPKLWA TAVDFSTQGV TICFESSWGN GNFTAPLVGS FNATNLLLAL ATLLVSGHSL PQLLAVAPRL QAVIGRMEVF QAPQADKAMM VVDYAHTPDA LDKALQALRV HCDGQLWCLF GCGGDRDSGK RPMMAAIAEQ YADHIILVDD NPRSEDPQQI MLDMQAGLTV ATAATIIHDR AQACAYALTH AKANDIILVA GKGHEDYQIL ADRTIHYSDR ETVAALFREL P //