ID   DSBB_VIBCH              Reviewed;         173 AA.
AC   Q9KQU6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=VC_1902;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
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DR   EMBL; AE003852; AAF95050.1; -; Genomic_DNA.
DR   PIR; H82141; H82141.
DR   RefSeq; NP_231536.1; NC_002505.1.
DR   RefSeq; WP_001221803.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KQU6; -.
DR   SMR; Q9KQU6; -.
DR   STRING; 243277.VC_1902; -.
DR   DNASU; 2613531; -.
DR   EnsemblBacteria; AAF95050; AAF95050; VC_1902.
DR   GeneID; 57740535; -.
DR   KEGG; vch:VC_1902; -.
DR   PATRIC; fig|243277.26.peg.1818; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_098660_2_0_6; -.
DR   OMA; GGALYMQ; -.
DR   BioCyc; VCHO:VC1902-MON; -.
DR   Proteomes; UP000000584; 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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..173
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000059361"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        17..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        34..51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        52..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        68..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        75..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        93..147
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        167..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        43..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        107..133
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ   SEQUENCE   173 AA;  19334 MW;  3B159DD2CA28D53B CRC64;
     MRILSSLKTF SQSRLSWLLL LAFVVFFTLC AMYFQHVMLL APCVMCIYER IAMLGIGVAA
     LIGAIAPQNP VVRWLGFAAW GASSYKGLML AIEHVNYQFN PSPFATCDLF VTFPAWAPLN
     QWAPNLFEAY GDCSKVVWQF LTLSMPQWLV VIFAANLLAL AIFVVAQLAK TSR