ID   DSBB_LEGPL              Reviewed;         163 AA.
AC   Q5WT71;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=lpl2654;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH16895.1; -; Genomic_DNA.
DR   RefSeq; WP_011216590.1; NC_006369.1.
DR   AlphaFoldDB; Q5WT71; -.
DR   EnsemblBacteria; CAH16895; CAH16895; lpl2654.
DR   KEGG; lpf:lpl2654; -.
DR   LegioList; lpl2654; -.
DR   HOGENOM; CLU_098660_1_1_6; -.
DR   OMA; GGALYMQ; -.
DR   Proteomes; UP000002517; 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..163
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000298365"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        10..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        27..44
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        45..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        59..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        65..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        83..139
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   TOPO_DOM        159..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        36..39
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT   DISULFID        98..125
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ   SEQUENCE   163 AA;  18303 MW;  3C61358AFE78EDB0 CRC64;
     MKKLTYRKIQ SFQAIITVLV IFASFYLEYA AGLQPCPLCL MQRVCVFILL GLMGVSLGTV
     KKAHIVSLIQ FQVACAGLYF SLRQLWLQSL PSDQAPACMP GLDVLIQYFP WQTVAKALFW
     GAGDCAEVTW TMFGVSMPGW AAMYFLSMAI MGLFLFFRTR TIN