ID   UPPP1_OENOB             Reviewed;         278 AA.
AC   Q04FK3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-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=OEOE_0848;
OS   Oenococcus oeni (strain BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Lactobacillales; Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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 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   -!- SIMILARITY: Belongs to the uppP family.
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DR   EMBL; CP000411; ABJ56769.1; -; Genomic_DNA.
DR   RefSeq; YP_810434.1; -.
DR   GeneID; 4416107; -.
DR   GenomeReviews; CP000411_GR; OEOE_0848.
DR   KEGG; ooe:OEOE_0848; -.
DR   NMPDR; fig|203123.1.peg.8; -.
DR   OMA; Q04FK3; IYGIAFI.
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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Transmembrane.
FT   CHAIN         1    278       Undecaprenyl-diphosphatase 1.
FT                                /FTId=PRO_0000290739.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     43     63       Potential.
FT   TRANSMEM     83    103       Potential.
FT   TRANSMEM    112    132       Potential.
FT   TRANSMEM    192    212       Potential.
FT   TRANSMEM    224    244       Potential.
FT   TRANSMEM    257    277       Potential.
SQ   SEQUENCE   278 AA;  30998 MW;  5661E2C62C6892F4 CRC64;
     MFFGILKAII LGIVEGITEF LPISSTGHLI IVDQFVKISS NKAFTTTFEY VIQLGAIIAV
     VLLYWKRLWP FGGGKTEKQR FNIWATWVKV VVGVIPSVII GFLLNDWMDK HLMNWLVVSI
     ALIVYGIAFI FIENYQKNRR PRVRTINHLT LADVLKIGFF QVLSIVPGTS RSGATILGGI
     SIGVSREAAA EFSFFLSIPT MLGVSVLKIG SYLHSHGMFS GEQIVILLVG MFVSFVVAYV
     VIKWLLRFIQ THDFKAFGWY RIILGVLVIA LGAIGIID
//