ID A0A5P6VNR3_PSEXY Unreviewed; 490 AA. AC A0A5P6VNR3; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 17-JUN-2020, entry version 2. DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|SAAS:SAAS00766893}; DE EC=6.3.2.- {ECO:0000256|SAAS:SAAS00951511}; GN ORFNames=FXF36_03790 {ECO:0000313|EMBL:QFJ54052.1}; OS Pseudobutyrivibrio xylanivorans. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Pseudobutyrivibrio. OX NCBI_TaxID=185007 {ECO:0000313|EMBL:QFJ54052.1, ECO:0000313|Proteomes:UP000327030}; RN [1] {ECO:0000313|EMBL:QFJ54052.1, ECO:0000313|Proteomes:UP000327030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MA3014 {ECO:0000313|EMBL:QFJ54052.1, RC ECO:0000313|Proteomes:UP000327030}; RA Palevich N., Maclean P.H., Kelly W.J., Leahy S.C., Rakonjac J., RA Attwood G.T.; RT "Complete Genome Sequence of the Polysaccharide-Degrading Rumen Bacterium RT Pseudobutyrivibrio xylanivorans MA3014."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135, CC ECO:0000256|SAAS:SAAS00951526}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000256|SAAS:SAAS00569976}. 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; CP043028; QFJ54052.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000327030; Chromosome 1. 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; 3.90.190.20; -; 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|SAAS:SAAS00951530}; KW Cell cycle {ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553}; KW Cell division {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951537}; KW Cell shape {ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951523}; Cytoplasm {ECO:0000256|SAAS:SAAS00951519}; KW Ligase {ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:QFJ54052.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00951542}; KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951548}. FT DOMAIN 22..90 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 108..309 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 329..414 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" SQ SEQUENCE 490 AA; 54250 MW; 2BC958A03A474C20 CRC64; MKLVELLDKL NYELYAGELD REISTLTYDS RKVEKDSVFV CISGTVRDAH DFIPDVIEKG ASVIIIEKDV EPVDGITYIK VKNSREALAY TSAAYFGHPA EKLKTIGITG TKGKTTTTYM VKSILDSAGI KTGLIGTIES IVGDERIPAV NTTPESYRVQ ELFAQMVEAG LDAVVMEVSS QALMLHRVSG FTFDIGVFTN LEPDHIGDNE HKDFEDYMYC KSLLFQQCKT GIFNGDSEHI EGILKGHTCE VIKYGYGKDN DLIAENVELL NENGALGVRY HITGKEDMTV EVNVPGAFSV YNSLTAVAIC KQFNVAEDKI KSALMNVHVK GRIELVPVSS KFTVMIDYAH NAMALESLLT TLRAYEPGRL VCMFGCGGNR AKSRRYEMGE VSSKLADLTV VTSDNPRNEE PMDIINDILI GVKKADGEYV TVPDRKEAIR YCLTNAKDGD IIVLAGKGHE DYQEIKGVKH HMDERELIAE IIKEDGNDII //