ID UPPP1_BURCM Reviewed; 276 AA. AC Q0BHM0; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Undecaprenyl-diphosphatase 1; DE EC=3.6.1.27; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 1; DE AltName: Full=Bacitracin resistance protein 1; GN Name=uppP1; OrderedLocusNames=Bamb_0794; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) 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: Undecaprenyl diphosphate + H(2)O = CC undecaprenyl phosphate + phosphate. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein (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 -!- SIMILARITY: Belongs to the uppP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000440; ABI86353.1; -; Genomic_DNA. DR RefSeq; YP_772687.1; -. DR GeneID; 4308977; -. DR GenomeReviews; CP000440_GR; Bamb_0794. DR KEGG; bam:Bamb_0794; -. DR NMPDR; fig|339670.3.peg.3020; -. DR OMA; Q0BHM0; RWLLRYI. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:HAMAP. DR GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR HAMAP; MF_01006; -; 1. DR InterPro; IPR003824; Bacitracin-R_BacA. DR Pfam; PF02673; BacA; 1. DR TIGRFAMs; TIGR00753; undec_PP_bacA; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Hydrolase; KW Membrane; Peptidoglycan synthesis; Transmembrane. FT CHAIN 1 276 Undecaprenyl-diphosphatase 1. FT /FTId=PRO_0000290693. FT TRANSMEM 4 24 Potential. FT TRANSMEM 45 62 Potential. FT TRANSMEM 83 103 Potential. FT TRANSMEM 108 128 Potential. FT TRANSMEM 187 207 Potential. FT TRANSMEM 217 237 Potential. FT TRANSMEM 252 272 Potential. SQ SEQUENCE 276 AA; 30303 MW; FAE8690EC2AD0CD9 CRC64; MDWILICKAL ILGVVEGLTE FLPVSSTGHL IVAGSFLNFN DAHAKTFDVV IQFGAILAVC WEYRQRIVSI VTGLPSRPDA QRFTLNVVIA TIPAIALGLL FEKKIKAVLF SPVPVAFALV VGGAIILWAE ARQRERREPP RVQSIDALTP LDALKVGLAQ CFALVPGMSR SGSTIIGGML FGLDRRVATE FSFFLAIPII FGATLYETVK DWQAFTVDSL GLFALGLVAA FVSAFVCVRW LLRFVATHDF TVFAWYRIAF GLFVLLVGYS GWLNWA //