(data stored in ACNUC7421 zone)

SWISSPROT: UPPP_RHOPS

ID   UPPP_RHOPS              Reviewed;         268 AA.
AC   Q13ES7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JAN-2019, entry version 79.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006};
GN   OrderedLocusNames=RPD_0172;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl
CC       diphosphate (UPP). Confers resistance to bacitracin.
CC       {ECO:0000255|HAMAP-Rule:MF_01006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC         trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392;
CC         EC=3.6.1.27; Evidence={ECO:0000255|HAMAP-Rule:MF_01006};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01006}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01006}.
DR   EMBL; CP000283; ABE37412.1; -; Genomic_DNA.
DR   RefSeq; WP_011500604.1; NC_007958.1.
DR   STRING; 316057.RPD_0172; -.
DR   EnsemblBacteria; ABE37412; ABE37412; RPD_0172.
DR   KEGG; rpd:RPD_0172; -.
DR   eggNOG; ENOG4105DWR; Bacteria.
DR   eggNOG; COG1968; LUCA.
DR   HOGENOM; HOG000218356; -.
DR   KO; K06153; -.
DR   OMA; PDARMGW; -.
DR   OrthoDB; 1826154at2; -.
DR   BioCyc; RPAL316057:RPD_RS00865-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; 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-UniRule.
DR   HAMAP; MF_01006; Undec_diphosphatase; 1.
DR   InterPro; IPR003824; UppP.
DR   PANTHER; PTHR30622; PTHR30622; 1.
DR   Pfam; PF02673; BacA; 1.
DR   TIGRFAMs; TIGR00753; undec_PP_bacA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13ES7.
DR   SWISS-2DPAGE; Q13ES7.
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN         1    268       Undecaprenyl-diphosphatase.
FT                                /FTId=PRO_0000290757.
FT   TRANSMEM     47     67       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM     83    103       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM    109    129       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM    144    164       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM    184    204       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM    218    238       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
FT   TRANSMEM    246    266       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01006}.
SQ   SEQUENCE   268 AA;  29365 MW;  CA64F4CB89AC039E CRC64;
     MLFDIFRAVI LGVVEGVTEF LPVSSTGHLL LVGRFFNLGE DSFWKSFAVL IQLGAILAIL
     SIYFAKLWRI ALGMFSDPAA RRFVIGVLVA FLPAAMIGAV AGSYIKLYLF NPWVVCFSLI
     VGGAILLWVD QLDLNPQQHD ATAFPLPMYF YIGCAQCLAM IPGVSRSGAS IVAAMLFGAD
     KRSAAEFSFF LAIPTMVGAF VYDFYKNRGE MTTDHLTIVA IGFVVSFITA VIVVKTFLGY
     VTRHGFELFA WWRVIVGTLG LIALAMGR
//

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