DSBB_SHEON
ID DSBB_SHEON Reviewed; 175 AA.
AC P59346;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SO_2887;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55903.1; -; Genomic_DNA.
DR RefSeq; NP_718459.1; NC_004347.2.
DR RefSeq; WP_011072798.1; NZ_CP053946.1.
DR AlphaFoldDB; P59346; -.
DR STRING; 211586.SO_2887; -.
DR PaxDb; P59346; -.
DR KEGG; son:SO_2887; -.
DR PATRIC; fig|211586.12.peg.2786; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_098660_2_0_6; -.
DR OMA; GGALYMQ; -.
DR OrthoDB; 1859420at2; -.
DR PhylomeDB; P59346; -.
DR BioCyc; SONE211586:G1GMP-2665-MON; -.
DR Proteomes; UP000008186; 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; 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..175
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000059358"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 14..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 31..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 49..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 65..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 90..144
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 145..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 164..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 40..43
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 104..130
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ SEQUENCE 175 AA; 19484 MW; 7E3BCF1A47A7ECB8 CRC64;
MTAFTRFAHS RVSWFFLTGS AIALEAAALY FQYVMKLDPC VMCIYQRLAV FGILAAGLVG
MTAPKYRIIR ILGVLGWAIS ATWGLKLALA LVDMQNNPSP FSTCSFLPEF PAWMPLHEWF
PAIMLPTGMC TDVPWQFIGV TMAEWMVVAF SGYLVVLLLF IVPILSGSNK PSLYK