ID   UPPP2_BURTA             Reviewed;         276 AA.
AC   Q2SUY6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Undecaprenyl-diphosphatase 2;
DE            EC=3.6.1.27;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase 2;
DE   AltName: Full=Bacitracin resistance protein 2;
GN   Name=uppP2; OrderedLocusNames=BTH_I2750;
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; ABC36529.1; -; Genomic_DNA.
DR   RefSeq; YP_443263.1; -.
DR   GeneID; 3847177; -.
DR   GenomeReviews; CP000086_GR; BTH_I2750.
DR   KEGG; bte:BTH_I2750; -.
DR   TIGR; BTH_I2750; -.
DR   HOGENOM; Q2SUY6; -.
DR   OMA; Q2SUY6; FALLWYF.
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.
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 2.
FT                                /FTId=PRO_0000250229.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     44     64       Potential.
FT   TRANSMEM     87    107       Potential.
FT   TRANSMEM    114    134       Potential.
FT   TRANSMEM    150    170       Potential.
FT   TRANSMEM    190    210       Potential.
FT   TRANSMEM    222    242       Potential.
FT   TRANSMEM    251    271       Potential.
SQ   SEQUENCE   276 AA;  30265 MW;  280F6D50F9DB3276 CRC64;
     MSLWFLVFLS VLQGVTELFP VSSLGHTLLV PALFGMHIDK HAPQLLPFLV ALHLGTAFAL
     LWYFRERWIA LIAGFFASLN GRKNDEGHLM WALIIGTIPA GLVGLLLEKR IERVFHDLRI
     VAVALIVNGI LLWLGDRIQR ARAHRPPEKL TFKQAFFVGL AQVGALIPGF SRSGLTMIAG
     NAAGLTAEKA AEFSFLLGTP IIFAAGLLEL PKLFHAPDQL ADALLGGVLT AIAAYLSVRF
     LMRYFEGRGR LASFGLYCAL AGLFCLGWFM FHAQPV
//