ID   UPPP2_OENOB             Reviewed;         271 AA.
AC   Q04D15;
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 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=OEOE_1821;
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; ABJ57657.1; -; Genomic_DNA.
DR   RefSeq; YP_811322.1; -.
DR   GeneID; 4415374; -.
DR   GenomeReviews; CP000411_GR; OEOE_1821.
DR   KEGG; ooe:OEOE_1821; -.
DR   NMPDR; fig|203123.1.peg.193; -.
DR   OMA; Q04D15; ANGMILL.
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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Transmembrane.
FT   CHAIN         1    271       Undecaprenyl-diphosphatase 2.
FT                                /FTId=PRO_0000290740.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     46     66       Potential.
FT   TRANSMEM     88    108       Potential.
FT   TRANSMEM    111    131       Potential.
FT   TRANSMEM    146    166       Potential.
FT   TRANSMEM    190    210       Potential.
FT   TRANSMEM    220    240       Potential.
FT   TRANSMEM    251    271       Potential.
SQ   SEQUENCE   271 AA;  29785 MW;  0D102F988A22A78B CRC64;
     MNFFQAIILA IAQGVSELFP ISSVAHSVII PYLFGWKLSP FFLKTNFLEF VVMMHIGTTI
     SLIVYFRKDW KKMLKSLFNK KTSKRNLALI VIGTIPAIIL GAIFEQTITN AFSDVIVASI
     FLIFNGLLLF FGEQTKKRGN KSIEDLKGWQ ALVIGCFQSL ALIPGFSRSG SSITAGFWMG
     LSNEESARFS MLLSTPMVAG AATLEIPKLI KNHVPGLLSL SLIGGIVAGL AAFLSIYILM
     HWFNHKKNNT MLPFAIYCIV IGIGVLASKA I
//