ID   UPPP2_BURCM             Reviewed;         276 AA.
AC   Q0BGG1;
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 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=Bamb_1204;
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.
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DR   EMBL; CP000440; ABI86762.1; -; Genomic_DNA.
DR   RefSeq; YP_773096.1; -.
DR   GeneID; 4309935; -.
DR   GenomeReviews; CP000440_GR; Bamb_1204.
DR   KEGG; bam:Bamb_1204; -.
DR   NMPDR; fig|339670.3.peg.2337; -.
DR   OMA; Q0BGG1; 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_0000290694.
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    220    240       Potential.
FT   TRANSMEM    251    271       Potential.
SQ   SEQUENCE   276 AA;  30338 MW;  5BE56E3B9DC83E26 CRC64;
     MSLWFLVFLS VLQGVTELFP VSSLGHTLLV PALFGMHIDK HAPQLLPFLV ALHLGTALAL
     LWYFRARWIA LISGFFAQLG GRKNDDGHLM WALIIGTIPT GIVGLLLEKR LERVFHDLRI
     VAVALIINGV LLWVGDRIQR SRAHQAPEKM TFKQAFFVGL AQIGALIPGF SRSGLTMIAG
     NVAGLTAEKA AEFSFLLGTP IIFAAGVLEL PKLFHARDQL MDALLGGVLT AIAAYLSVRF
     LMRYFEGRGR LASFGVYCVI AGVFFLGWFM LHPQPV
//