ID   DSBB_BURCE              Reviewed;         170 AA.
AC   P94287;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Disulfide bond formation protein B;
DE   AltName: Full=Disulfide oxidoreductase;
GN   Name=dsbB;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KF1;
RX   PubMed=8926116; DOI=10.1128/iai.64.10.4378-4380.1996;
RA   Abe M., Nakazawa T.;
RT   "The dsbB gene product is required for protease production by Burkholderia
RT   cepacia.";
RL   Infect. Immun. 64:4378-4380(1996).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by oxidizing the DsbA protein (By similarity). Required
CC       for the production of extracellular protease. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000305}.
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DR   EMBL; D83234; BAA11858.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94287; -.
DR   SMR; P94287; -.
DR   STRING; 292.DM42_808; -.
DR   eggNOG; COG1495; Bacteria.
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 reductase 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;
KW   Cell inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW   Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..170
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000059341"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..144
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..44
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..130
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  18765 MW;  BCC1918444BDFC6B CRC64;
     MNDYTLALRR ERRLLMLLGW VCIALLAGAL YLQYVKNEDP CPLCIIQRYF FCAIGIFAFV
     AAGIRNWRGV WVLELLIAIA AAGGVGTAAR HLSIQMNPGF SCGFDTLQPI VDSLPPAQWF
     PGMFKVAGLC ETVYPPIFGI LLPGWALIGF AVILVAVVAS LWRHRRKLAS