DSBB_PSESM
ID DSBB_PSESM Reviewed; 169 AA.
AC Q887H2;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-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=PSPTO_1324;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54846.1; -; Genomic_DNA.
DR RefSeq; NP_791151.1; NC_004578.1.
DR RefSeq; WP_005764026.1; NC_004578.1.
DR AlphaFoldDB; Q887H2; -.
DR SMR; Q887H2; -.
DR STRING; 223283.PSPTO_1324; -.
DR EnsemblBacteria; AAO54846; AAO54846; PSPTO_1324.
DR GeneID; 1182960; -.
DR KEGG; pst:PSPTO_1324; -.
DR PATRIC; fig|223283.9.peg.1346; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_098660_1_0_6; -.
DR OMA; GGALYMQ; -.
DR OrthoDB; 1859420at2; -.
DR PhylomeDB; Q887H2; -.
DR Proteomes; UP000002515; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..169
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000059354"
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..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..169
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 102..130
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ SEQUENCE 169 AA; 18213 MW; BBE0C6D229B258D2 CRC64;
MSNDTFYLKR EKRFLVLLGI ICLSLIGGAL YMQIALGEAP CPLCILQRYA LLFIAIFAFI
GAAMNGRRGV TVFEALVTLS ALCGIAAAGR HAWILAHPSD SCGIDILQPI VDGLPLATLF
PTGFQVSGFC TTPYPPVLGL SLAQWALTAF VLTAILVPAC IIRNRRKPY
