(data stored in ACNUC7421 zone)

SWISSPROT: D4YXJ5_SPHJU

ID   D4YXJ5_SPHJU            Unreviewed;       269 AA.
AC   D4YXJ5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 44.
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=bacA {ECO:0000313|EMBL:BAI95077.1};
GN   Synonyms=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN   OrderedLocusNames=SJA_C1-02430 {ECO:0000313|EMBL:BAI95077.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95077.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95077.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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 inner 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; AP010803; BAI95077.1; -; Genomic_DNA.
DR   RefSeq; WP_013038881.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02430; -.
DR   EnsemblBacteria; BAI95077; BAI95077; SJA_C1-02430.
DR   GeneID; 29271947; -.
DR   KEGG; sjp:SJA_C1-02430; -.
DR   eggNOG; ENOG4105DWR; Bacteria.
DR   eggNOG; COG1968; LUCA.
DR   HOGENOM; HOG000218356; -.
DR   KO; K06153; -.
DR   OMA; PDARMGW; -.
DR   OrthoDB; POG091H00ZR; -.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YXJ5.
DR   SWISS-2DPAGE; D4YXJ5.
KW   Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702335};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01006};
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:UP000007753};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702354, ECO:0000313|EMBL:BAI95077.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000007753};
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     40     63       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM     83    102       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    114    133       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    145    164       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    184    205       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    217    240       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    252    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
SQ   SEQUENCE   269 AA;  29219 MW;  35F86A993BF789D1 CRC64;
     MDLHYLTVIL LGIVEGLTEF LPVSSTGHLI LASELLGYDA STWAMFNVVI QLGAILAVVV
     LYWRTFWAVG MGLLRREPAS WRFLRNLLVA FIPAAVIGLA LHNYIEELLG APRVVAWALI
     AGGIAILGIE RMVKENRFHG IADIPFVRVV GIGFIQCLAM IPGISRSGAT IMGALTLGVE
     RRTAAEFSFF LAIPTMLGAT TLELLKNGDK LTSATVGWGS IVLGFIVSFI VALLVIKWFV
     GLVSRHGFAP FAWYRIVAGI AALAWLSLR
//

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