ID   UPPP1_RHORT             Reviewed;         282 AA.
AC   Q2RYH3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Rru_A0017;
OS   Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
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., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-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; CP000230; ABC20822.1; -; Genomic_DNA.
DR   RefSeq; YP_425109.1; -.
DR   GeneID; 3833905; -.
DR   GenomeReviews; CP000230_GR; Rru_A0017.
DR   KEGG; rru:Rru_A0017; -.
DR   NMPDR; fig|1085.1.peg.1097; -.
DR   HOGENOM; Q2RYH3; -.
DR   OMA; Q2RYH3; FTRYSSS.
DR   BioCyc; RRUB269796:RRU_A0017-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.
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    282       Undecaprenyl-diphosphatase 1.
FT                                /FTId=PRO_0000250258.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     46     66       Potential.
FT   TRANSMEM     91    111       Potential.
FT   TRANSMEM    117    137       Potential.
FT   TRANSMEM    150    170       Potential.
FT   TRANSMEM    193    213       Potential.
FT   TRANSMEM    226    246       Potential.
FT   TRANSMEM    260    280       Potential.
SQ   SEQUENCE   282 AA;  29284 MW;  629AEA2194B2B7AE CRC64;
     MLLLQIVVLA LIQGITEVLP LSSTGHLALL PLLTPWPSPT TWPDQGVALD VAVHLGTLGA
     VALYFWRDEA AMIGGCLRLL KGKRDPGARL AFLVVLGTLP AVATVLLLAH FAGPIASPGL
     ATIGWTTLGF GLLLGVIDRL CMTVKRVEHM GGIDCLLIGL AQCLALLPGV SRTGVAMTAA
     RLLGYERVES ARFSMLLSIP AIAGAATLVG LDLARVGQSA MAPAALIAAV TAFLAAFLAV
     AAMMAWLRRH GFGPFVAYRV LLGAALLALA YLGPDLAPFL VS
//