ID A0A014KZP4_9ACTO Unreviewed; 278 AA. AC A0A014KZP4; 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=Z951_41335; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1158056; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRh5; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of RT Streptomyces sp. PRh5, a strain for production of geldanamycin, RT nigericin and nocardamine."; 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; JABQ01000103; EXU62476.1; -; 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 46 66 Helical; (By similarity). FT TRANSMEM 95 115 Helical; (By similarity). FT TRANSMEM 119 139 Helical; (By similarity). FT TRANSMEM 153 173 Helical; (By similarity). FT TRANSMEM 191 211 Helical; (By similarity). FT TRANSMEM 225 245 Helical; (By similarity). FT TRANSMEM 256 276 Helical; (By similarity). SQ SEQUENCE 278 AA; 29085 MW; F672AC00A27DEDC8 CRC64; MSAISIGQAA VLGIVEGITE FLPVSSTGHL KITEGLMGIP VDDASVVGFT AVIQVGAIAA VLVYFFKDIV RIVSAWGRGL AHREQRYHHD YKFAWWVICA TIPIVIVGLA AKPLIEGPLA SLWVVAGSLV AGSGVMWVAD QMGRHKRGED DTGFKDAMLV GCSQILALLF PGFSRSGATM STALILDLDR VAATRLSFFL GIPALTGAGL YELKDAVGAG VGTAPLVVGT AVSFVVAYAS IAWLLKFVAK HSFNAFVVYR VAIGVLLLGL LGTGALTA //