DSBB_SHEDO
ID DSBB_SHEDO Reviewed; 175 AA.
AC Q12NQ9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Sden_1633;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
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}.
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DR EMBL; CP000302; ABE54917.1; -; Genomic_DNA.
DR RefSeq; WP_011496075.1; NC_007954.1.
DR AlphaFoldDB; Q12NQ9; -.
DR SMR; Q12NQ9; -.
DR STRING; 318161.Sden_1633; -.
DR EnsemblBacteria; ABE54917; ABE54917; Sden_1633.
DR KEGG; sdn:Sden_1633; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_098660_2_0_6; -.
DR OMA; GGALYMQ; -.
DR OrthoDB; 1859420at2; -.
DR Proteomes; UP000001982; 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..175
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000298407"
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; 19835 MW; 077FF7CCBD1FC7B9 CRC64;
MSKLVTFSQQ RSAWLILMFS ALGLEASALY FQYVMLLDPC VMCIYIRVAV LGLILAGLVG
SIAPRFWIVR FLGMSLWGVS SAWGAKLSFE LYQMQANPSP FSTCSFYPEF PTWMPLDAWM
PSIFMPTGMC SDIPWTMMSL SMTQWTLIAF VGYSIAFLLF IYPGLLYKKP TNPYS