(data stored in ACNUC7421 zone)

SWISSPROT: DSBB_ALCBS

ID   DSBB_ALCBS              Reviewed;         167 AA.
AC   Q0VSY8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 83.
DE   RecName: Full=Disulfide bond formation protein B {ECO:0000255|HAMAP-Rule:MF_00286};
DE   AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00286};
GN   Name=dsbB {ECO:0000255|HAMAP-Rule:MF_00286}; OrderedLocusNames=ABO_0262;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by oxidizing the DsbA protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00286}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00286}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00286}.
CC   -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00286}.
DR   EMBL; AM286690; CAL15710.1; -; Genomic_DNA.
DR   RefSeq; WP_011587558.1; NC_008260.1.
DR   STRING; 393595.ABO_0262; -.
DR   EnsemblBacteria; CAL15710; CAL15710; ABO_0262.
DR   KEGG; abo:ABO_0262; -.
DR   eggNOG; ENOG41080I0; Bacteria.
DR   eggNOG; COG1495; LUCA.
DR   HOGENOM; HOG000218136; -.
DR   KO; K03611; -.
DR   OMA; GGALYMQ; -.
DR   OrthoDB; 1859420at2; -.
DR   BioCyc; ABOR393595:ABO_RS01330-MONOMER; -.
DR   Proteomes; UP000008871; 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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1550.10; -; 1.
DR   HAMAP; MF_00286; DsbB; 1.
DR   InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR   InterPro; IPR022920; Disulphide_bond_form_DsbB.
DR   InterPro; IPR023380; DsbB-like_sf.
DR   Pfam; PF02600; DsbB; 1.
DR   SUPFAM; SSF158442; SSF158442; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0VSY8.
DR   SWISS-2DPAGE; Q0VSY8.
KW   Cell inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW   Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..167
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000298336"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        12..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        29..46
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        47..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        64..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        71..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        88..144
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        145..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        164..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        38..41
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        103..130
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ   SEQUENCE   167 AA;  17568 MW;  4104B6E49EA1F4AC CRC64;
     MSSIIPAPRP LNALAFLACL AAIVGALYLQ HVDGLEPCPL CIFQRVGVIA GAVILLIASL
     HGPKNIGVRI YGALTTLAAL GGGAVAARHI WLQNLPADQV PACGPGLDYM LEVFPLQNVL
     QQVLAGSGEC AEMDWSFLGL SLPGWSMVVF AGLLLVGLIQ MFRPLTR
//

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