ID   DSBB_PSYCK              Reviewed;         176 AA.
AC   Q1QES7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Pcryo_0042;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000323; ABE73826.1; -; Genomic_DNA.
DR   RefSeq; WP_011512418.1; NC_007969.1.
DR   AlphaFoldDB; Q1QES7; -.
DR   SMR; Q1QES7; -.
DR   STRING; 335284.Pcryo_0042; -.
DR   KEGG; pcr:Pcryo_0042; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_098660_1_1_6; -.
DR   OMA; GGALYMQ; -.
DR   Proteomes; UP000002425; 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 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..176
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000298397"
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..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        89..145
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        146..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        165..176
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        104..131
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ   SEQUENCE   176 AA;  19655 MW;  051BBBD26F77F5ED CRC64;
     MLQLTTYRNL QVFLVIMTAI GMSFALFFLQ RYMGFSPCPL CIFQRIGLMI MGGFALIAAL
     FHPKSMVIRL LLWLGSLAGI GWAAIVAGRH VWLQHLPADQ VPSCGPGLDY WLDTLPMQQV
     LKEVFAGSGE CASIDWTFLG LSIPEQSLIL FSILILTHLL ILWRIVRPAT PKPLAR