ID   UPPP2_PSEPF             Reviewed;         277 AA.
AC   Q3K9J0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=Pfl01_3826;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyripides N., Anderson I., Richardson P.;
RT   "Complete sequence of Pseudomonas fluorescens PfO-1.";
RL   Submitted (AUG-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; CP000094; ABA75564.1; -; Genomic_DNA.
DR   RefSeq; YP_349555.1; -.
DR   GeneID; 3714854; -.
DR   GenomeReviews; CP000094_GR; Pfl01_3826.
DR   KEGG; pfo:Pfl01_3826; -.
DR   HOGENOM; Q3K9J0; -.
DR   OMA; Q3K9J0; ADTIHEY.
DR   BioCyc; PFLU205922:PFL_3826-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    277       Undecaprenyl-diphosphatase 2.
FT                                /FTId=PRO_0000227631.
FT   TRANSMEM     43     63       Potential.
FT   TRANSMEM     87    107       Potential.
FT   TRANSMEM    109    129       Potential.
FT   TRANSMEM    183    203       Potential.
FT   TRANSMEM    214    234       Potential.
FT   TRANSMEM    254    274       Potential.
SQ   SEQUENCE   277 AA;  30394 MW;  3454560A3AACE8EF CRC64;
     MDLLTLFKVL ILGAVEGLTE FLPISSTGHQ IIVADLLEFG GERAMAFNII IQLGAILAVV
     WEFRPKIFEI VKGLPTQSNA QRFTRNLLIA FFPAVILGVL FADTIHEYLF NPITVAVALV
     VGGIVMLWAE QRDHVVSVDH VDDMKWADAL KIGCVQCLAM IPGTSRSGST IIGGLLFGLS
     RKAATEFSFF LAMPTMVGAA VYSGYKYREL FQSSDLPVFA LGFVVAFIFA MIAVRGLLKF
     IANHSYATFA WYRIAFGLLI LATWQFGWVN WTAAAAA
//