ID   DSBB_HAEI8              Reviewed;         177 AA.
AC   Q4QNB7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=NTHI0552;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87480.1; -; Genomic_DNA.
DR   RefSeq; WP_011272043.1; NC_007146.2.
DR   AlphaFoldDB; Q4QNB7; -.
DR   SMR; Q4QNB7; -.
DR   EnsemblBacteria; AAX87480; AAX87480; NTHI0552.
DR   KEGG; hit:NTHI0552; -.
DR   HOGENOM; CLU_098660_2_0_6; -.
DR   OMA; GGALYMQ; -.
DR   OrthoDB; 1859420at2; -.
DR   Proteomes; UP000002525; 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..177
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000298360"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        15..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        32..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        50..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        66..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        73..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        91..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..177
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        41..44
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        105..131
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ   SEQUENCE   177 AA;  20384 MW;  99BEE19791DCCDA7 CRC64;
     MLALLKQFSE KRFVWFLLAF SSLALESTAL YFQYGMGLQP CVLCVYERLA MIGLFVAGII
     ALLQPLAFIL RLIALALGLF SSIKGLLISF RHLDLQMNPA PWKQCEFIPN FPETLPFHQW
     FPFIFNPTGS CNESQWSLFG LTMVQWLVVI FSLYVVILTL LLIAQVIKTR KQRRLFN