DSBD_RALSO
ID DSBD_RALSO Reviewed; 608 AA.
AC Q8XV41;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 130.
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=RSc2990; ORFNames=RS01128;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD16699.1; -; Genomic_DNA.
DR RefSeq; WP_011002895.1; NC_003295.1.
DR AlphaFoldDB; Q8XV41; -.
DR SMR; Q8XV41; -.
DR STRING; 267608.RSc2990; -.
DR EnsemblBacteria; CAD16699; CAD16699; RSc2990.
DR GeneID; 60502497; -.
DR KEGG; rso:RSc2990; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_4; -.
DR OMA; CKEMERF; -.
DR Proteomes; UP000001436; 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:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..608
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007384"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 464..600
FT /note="Thioredoxin"
FT DISULFID 131..137
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 202..322
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 516..519
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 63189 MW; D8C3FF817F1E7460 CRC64;
MTLSAFLPLR RLLQLGLLLV AMATLALPAR AADDFLPPEQ AFRFSAVQID GQTVEVKFAI
ADGYYMYRER LAVAADPATV TFAPLELPPG KVKFDDTFNK DVETYRHALV FRVKAREAAS
PFSLIVTSQG CADQGVCYPP MKSRFRVEPA AASPAPPAAP LEAAGSSDAL GGRIASTLGG
GNLGAIAVLF LGLGLLLTFT PCVLPMLPIL SAIVVGEHAT RMRAAAVSVA YVLGMAVVYT
AVGVAAGLAG QGLQAALQNA WVLGAFAALM VVLSLAMFGL YELQLPAAWR HRLTQASNRL
SGGQVAGAAV MGALSALIVS PCVTPALAGA LAYIAQTGNA MVGGAALFSM SIGMGVPLVL
VGVGAGNLLP RAGYWLVVTK AIFGFILLGV ALWIVQPVLP AWLAMVAWAV LLIAAAVFLR
TFDSLPADAG PLPRLGKVVG VVLALAGAVQ LVGVAAGGRD PLQPLAGVMR ASAGAQPDAR
GVVFQRVKSV SEVDEAVRAA TATGRPVMLD FYADWCVSCK EMERLTFTDA RVRAALADVV
LLQADVTADG ADDRALLKRF SLFGPPATIF FDAQGNQAPV RVVGFERAET FLASLRRALG
TAQAKPST
