ID A0A014P5Q8_9BURK Unreviewed; 282 AA. AC A0A014P5Q8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 09-JUL-2014, entry version 2. DE RecName: Full=Undecaprenyl-diphosphatase; DE EC=3.6.1.27; DE AltName: Full=Bacitracin resistance protein; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase; GN Name=uppP; ORFNames=AX13_06845; OS Comamonas aquatica DA1877. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1457173; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA1877; RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P., RA Caudy A.A., Walhout A.J.; RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. RT elegans Gene Expression and Life History Traits."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl CC diphosphate (UPP). Confers resistance to bacitracin (By CC similarity). CC -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate + CC H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (By similarity). CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the CC inhibition of peptidoglycan synthesis by sequestering undecaprenyl CC diphosphate, thereby reducing the pool of lipid carrier available CC (By similarity). CC -!- SIMILARITY: Belongs to the UppP family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; JBOK01000002; EXU81510.1; -; Genomic_DNA. PE 3: Inferred from homology; KW Antibiotic resistance; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Membrane; KW Peptidoglycan synthesis; Transmembrane; Transmembrane helix. FT TRANSMEM 44 64 Helical; (By similarity). FT TRANSMEM 95 115 Helical; (By similarity). FT TRANSMEM 123 143 Helical; (By similarity). FT TRANSMEM 156 176 Helical; (By similarity). FT TRANSMEM 199 219 Helical; (By similarity). FT TRANSMEM 229 249 Helical; (By similarity). FT TRANSMEM 261 281 Helical; (By similarity). SQ SEQUENCE 282 AA; 30552 MW; 77D928B420F87E40 CRC64; MNATFGWLDA LILGLVQGLT EFLPISSSAH LRILGPLLPG GADPGAAFTA ITQLGTELAV LIYFRKDVLR MLVAWFASLP VIGSRRPGEA LHPDAKLAWL VILGTIPICV LGLLLRSWIE TTFRTLALTA VMLIVFGLLL GWAEKRSTQT RQIGQLGLRD GIVLGFAQAM ALIPGVSRSG GTITAGLLLG MTREAAARFS FLLAIPAVLL SGFYQLLFKR DPMSGEQWML TFMATAIAFV VGYAVIVWFM RLISNKGFGF FVIYRVLLGL AILAGLHFGF IQ //