(data stored in SCRATCH zone)

SWISSPROT: C1AST2_RHOOB

ID   C1AST2_RHOOB            Unreviewed;       282 AA.
AC   C1AST2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006,
GN   ECO:0000313|EMBL:BAH48864.1};
GN   OrderedLocusNames=ROP_06170 {ECO:0000313|EMBL:BAH48864.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48864.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48864.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48864.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl
CC       diphosphate (UPP). Confers resistance to bacitracin.
CC       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate +
CC       H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01006, ECO:0000256|SAAS:SAAS00702352}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01006}; Multi-pass membrane protein {ECO:0000256|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       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01006, ECO:0000256|SAAS:SAAS00702351}.
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DR   EMBL; AP011115; BAH48864.1; -; Genomic_DNA.
DR   STRING; 632772.ROP_06170; -.
DR   EnsemblBacteria; BAH48864; BAH48864; ROP_06170.
DR   KEGG; rop:ROP_06170; -.
DR   PATRIC; fig|632772.20.peg.676; -.
DR   eggNOG; ENOG4105DWR; Bacteria.
DR   eggNOG; COG1968; LUCA.
DR   HOGENOM; HOG000218357; -.
DR   KO; K06153; -.
DR   OMA; PDARMGW; -.
DR   OrthoDB; POG091H00ZR; -.
DR   Proteomes; UP000002212; 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-HAMAP.
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-HAMAP.
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; C1AST2.
DR   SWISS-2DPAGE; C1AST2.
KW   Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702335};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702333};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702357};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702339};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702354, ECO:0000313|EMBL:BAH48864.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702342};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702374};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702376};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702360}.
FT   TRANSMEM     92    110       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    122    142       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    191    209       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    229    248       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    260    281       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
SQ   SEQUENCE   282 AA;  30178 MW;  C104A987FF7447B1 CRC64;
     MMGEAMTWLQ AIVLGAVQGL TEFLPISSSG HLRIVSEIFF GDDAGASFTA VTQLGTEAAV
     LIYFARDIGR IIAGWFRGLF HAEHRSDLDY RMGWYVIIGT IPVGVLGFLF KDQIRTGARN
     LWLIATMLIV FALVIAAAEY YGRKVRPVED LRAKDGIIMG SAQALALIPG VSRSGGTISA
     GLFLGLTREA AARYSFLLAI PAVVASGLFS LPDAFEPAGE GLNASGPQLL VATVIAFAIG
     YASIAWLLRF VVDHSMYWFV GYRIILGVVV LSLLATGVVS AT
//

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