ID   UPPP1_BURTA             Reviewed;         276 AA.
AC   Q2SYE1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BTH_I1512;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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.
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DR   EMBL; CP000086; ABC37404.1; -; Genomic_DNA.
DR   RefSeq; YP_442058.1; -.
DR   GeneID; 3848646; -.
DR   GenomeReviews; CP000086_GR; BTH_I1512.
DR   KEGG; bte:BTH_I1512; -.
DR   TIGR; BTH_I1512; -.
DR   HOGENOM; Q2SYE1; -.
DR   OMA; Q2SYE1; IYGIAFI.
DR   BioCyc; BTHA271848:BTH_I1512-MON; -.
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_0000250228.
FT   TRANSMEM     85    105       Potential.
FT   TRANSMEM    108    128       Potential.
FT   TRANSMEM    187    207       Potential.
FT   TRANSMEM    217    237       Potential.
FT   TRANSMEM    253    273       Potential.
SQ   SEQUENCE   276 AA;  30296 MW;  D0FCCC3664D697DB CRC64;
     MDWILICKAL ALGIVEGLTE FLPVSSTGHL IVAGSFLRFH PEQAKTFDVV IQFGAILAVC
     WEYRRRIVDV VTGLPAQREA RRFTMNVVIA TLPAIALALL FEKTIKSVLF APVPVAVALV
     VGGAVILWVE GRQRERGKPS RVQSIDALTP LDALKVGLAQ CFALIPGVSR SGSTIIGGML
     FGLERRVATE FSFFLAIPVI FGATLYETAK DWHAFNVDSI GLFAIGLAAA FVSAFACVRW
     LLRYVASHDF TAFAWYRIVF GLFVLLVGYS GWIEWI
//