ID   UPPP1_PSEPF             Reviewed;         276 AA.
AC   Q3KD12;
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 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=Pfl01_2602;
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; ABA74343.1; -; Genomic_DNA.
DR   RefSeq; YP_348333.1; -.
DR   GeneID; 3714203; -.
DR   GenomeReviews; CP000094_GR; Pfl01_2602.
DR   KEGG; pfo:Pfl01_2602; -.
DR   HOGENOM; Q3KD12; -.
DR   OMA; Q3KD12; KPFAYYR.
DR   BioCyc; PFLU205922:PFL_2602-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    276       Undecaprenyl-diphosphatase 1.
FT                                /FTId=PRO_0000227630.
FT   TRANSMEM     43     63       Potential.
FT   TRANSMEM     85    105       Potential.
FT   TRANSMEM    109    129       Potential.
FT   TRANSMEM    184    204       Potential.
FT   TRANSMEM    214    234       Potential.
FT   TRANSMEM    254    274       Potential.
SQ   SEQUENCE   276 AA;  30315 MW;  95C1D6E85B689355 CRC64;
     MDLWTALQAL ILGVVEGLTE FLPISSTGHQ IIVADLLDFG GERAMAFNII IQLGAILAVV
     WEFRRKILDV VIGLPTQPSA RRFTANLLIA FLPAVVLGVI FADLIHHYLF NPITVAAALV
     VGGIVMLWAE QRQHEVHAET VDEIRWTDAL KIGFAQCLAM IPGTSRSGST IIGGLLFGLS
     RKTATEFSFF LAMPTMVGAA VYSGYKYRDL FVPADFPVFA IGFVTAFIFA MIAVRGLLKF
     IGSHSYAAFA WYRIVFGLVI LATWQFGWVD WTAAQP
//