DSBD_VIBCH
ID DSBD_VIBCH Reviewed; 600 AA.
AC Q9KNN1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Thiol:disulfide interchange protein DsbD;
DE EC=1.8.1.8;
DE AltName: Full=Protein-disulfide reductase;
DE Short=Disulfide reductase;
DE Flags: Precursor;
GN Name=dsbD; OrderedLocusNames=VC_2701;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Required to facilitate the formation of correct disulfide
CC bonds in some periplasmic proteins and for the assembly of the
CC periplasmic c-type cytochromes. Acts by transferring electrons from
CC cytoplasmic thioredoxin to the periplasm. This transfer involves a
CC cascade of disulfide bond formation and reduction steps (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000305}.
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DR EMBL; AE003852; AAF95841.1; -; Genomic_DNA.
DR PIR; A82043; A82043.
DR RefSeq; NP_232328.1; NC_002505.1.
DR RefSeq; WP_001259538.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KNN1; -.
DR SMR; Q9KNN1; -.
DR STRING; 243277.VC_2701; -.
DR DNASU; 2615529; -.
DR EnsemblBacteria; AAF95841; AAF95841; VC_2701.
DR GeneID; 57741295; -.
DR KEGG; vch:VC_2701; -.
DR PATRIC; fig|243277.26.peg.2577; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YYADWCV; -.
DR BioCyc; VCHO:VC2701-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 2.60.40.1250; -; 1.
DR HAMAP; MF_00399; DbsD; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR Pfam; PF11412; DsbC; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF74863; SSF74863; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..600
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007387"
FT TOPO_DOM 22..195
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..273
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..356
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..414
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..600
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 458..600
FT /note="Thioredoxin"
FT REGION 164..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..141
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 214..335
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 515..518
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 65210 MW; 23D01D76F730249C CRC64;
MRTLILCFSL LFALLTQPAW AIFGNNAGNN TGTASFAPTQ NRFVPVDEAF PFNAFQQGST
LFIDWQVKEG YYLYQDRISI SGENLEIGEY SLTEGEPYHD EFFGDVKIYT TPLSVPLPLV
AYQSGAKVIV QYQGCAKAGF CYPPETRVID ITPFNAESNR VIEPKTNTST QTTLPQTDNA
PTSAQDSLAN KLAQNWWTPL LFLALGVGLA FTPCVLPMYP ILTSIVLGGA QLTQRRALLL
SVIYVQGMAL TYTLLGLVVA SAGLQFQAAL QHPYVLMGLS VLFVALALSM FGLYSLQLPS
GVQTWLNSLS NAQQGGSLPG VFAMGAISGL VCSPCTTAPL SGALLYVAQS GDLLTGAVAL
YALAIGMGIP LILVAVFGNK LLPKAGNWME RVKTLFGFVL LAAPIFLLER IVPEFWSSVL
WSALGLAAFG WLYHVKNSLP FGGWKQSLIG IVAILGLLAS AQPLLNHWLA PTQTAQQVKQ
IQFTRIANLS ELQSALAEAK AQGKSVMLDF YADWCVACKE FEKYTFHAKQ VENKLSGFVL
LQADVTKNQP QDIELLKALN VLGLPTIEFW NAQGEPVPNA RITGFMAEQP FLDHLTQQGL
