ID   UPPP2_RHORT             Reviewed;         274 AA.
AC   Q2RTE2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Rru_A1803;
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; ABC22603.1; -; Genomic_DNA.
DR   RefSeq; YP_426890.1; -.
DR   GeneID; 3835227; -.
DR   GenomeReviews; CP000230_GR; Rru_A1803.
DR   KEGG; rru:Rru_A1803; -.
DR   NMPDR; fig|1085.1.peg.2377; -.
DR   HOGENOM; Q2RTE2; -.
DR   OMA; Q2RTE2; RWLLRYI.
DR   BioCyc; RRUB269796:RRU_A1803-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    274       Undecaprenyl-diphosphatase 2.
FT                                /FTId=PRO_0000250259.
FT   TRANSMEM     47     64       Potential.
FT   TRANSMEM     82    102       Potential.
FT   TRANSMEM    110    130       Potential.
FT   TRANSMEM    185    205       Potential.
FT   TRANSMEM    219    239       Potential.
FT   TRANSMEM    249    269       Potential.
SQ   SEQUENCE   274 AA;  29878 MW;  1D3EFC52D0925FE6 CRC64;
     MDLVMLIKAA ILGLVEGITE FLPISSTGHL IIAGSLLDFL DEQKRDVFVI VIQLGAILAV
     CWEYRRRLTD VVAGLGSDPQ SWKFVTNLLI AFLPAVVLGL TFGKAIKAHL FSPVPVATAF
     IVGGLVILWA ERRRHPIRVR EVDEMTWVDA LKIGLAQCFA LIPGTSRSGA TIIGGLFFGL
     SRKAATEFSF FLAIPTLTAA SLYDLYKNRA LLDGDMSGLM AVGFVVSFLS ALVAVRGLIR
     YISRHDFTVF AWYRIAFGLV VLATAWSGLV SWSA
//