DSBD_KLEP7
ID DSBD_KLEP7 Reviewed; 598 AA.
AC A6TH46;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399};
DE EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399};
DE AltName: Full=Protein-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE Short=Disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE Flags: Precursor;
GN Name=dsbD {ECO:0000255|HAMAP-Rule:MF_00399};
GN OrderedLocusNames=KPN78578_44560; ORFNames=KPN_04526;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00399}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00399}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00399}.
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DR EMBL; CP000647; ABR79880.1; -; Genomic_DNA.
DR RefSeq; WP_015959279.1; NC_009648.1.
DR AlphaFoldDB; A6TH46; -.
DR SMR; A6TH46; -.
DR STRING; 272620.KPN_04526; -.
DR EnsemblBacteria; ABR79880; ABR79880; KPN_04526.
DR KEGG; kpn:KPN_04526; -.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YRHRFQF; -.
DR Proteomes; UP000000265; 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..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 20..598
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_1000049611"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DOMAIN 459..598
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT REGION 147..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 122..128
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 216..338
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 513..516
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ SEQUENCE 598 AA; 64599 MW; E32B174BD62D1075 CRC64;
MAYRIITLIL LLCSTSATAG LFDAPGRSNF VPADQAFAFD FQQQQHDVNL SWQIKDGYYL
YRQQFTFSAA GATIDEPALP AGEWHEDEFY GKSEIFRQRL TVPVTVKEAD KEATLTVTWQ
GCADAGFCYP PETKVIPLSA VRAASNDGQA TAIEPMPSTS SRPAFNPPLP VEPRPAPELA
TSPAPAAVPP ADTPARLPFT ALWALLIGIG IAFTPCVLPM YPLISGIVLG GKQRLSTARA
LLLAFIYVQG MALTYTALGL VVAAAGLQFQ AALQHPYVLV GLSAVFILLA LSMFGLFTLQ
LPSSLQTRLT LLSNKRQGGS PGGVFAMGAI AGLICSPCTT APLSAILLYI AQSGNLWLGG
GTLYLYALGM GLPLILMTVF GNRLLPKSGP WMSHVKTAFG FVILALPVFL LERILGDQWG
LRLWSMLGVA FFSWAFITSL GATRPWMRLV QIILLAAALV SARPLQDWAF GAPAVEQQAH
LAFTRVSSVA ELDQALAQAK GQPVMLDLYA DWCVACKEFE KYTFSSPDVQ QALKGTVLLQ
VDVTKNSPQD VALLKHLQVL GLPTILFFNA EGQEQSERRV TGFMDAAAFS AHLRDWQA
