ID   DSBD_SHIBS              Reviewed;         565 AA.
AC   Q31T72;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
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}; OrderedLocusNames=SBO_4319;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB68736.1; -; Genomic_DNA.
DR   RefSeq; WP_011379353.1; NC_007613.1.
DR   AlphaFoldDB; Q31T72; -.
DR   SMR; Q31T72; -.
DR   EnsemblBacteria; ABB68736; ABB68736; SBO_4319.
DR   KEGG; sbo:SBO_4319; -.
DR   HOGENOM; CLU_014657_3_0_6; -.
DR   OMA; YYADWCV; -.
DR   Proteomes; UP000007067; 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; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   CHAIN           20..565
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000304396"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DOMAIN          434..565
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        122..128
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        182..304
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        480..483
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   565 AA;  61854 MW;  3ECE5005BAC9EB52 CRC64;
     MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL TWQIKDGYYL
     YRKQIRITPE HAKIADEQLP QGVWHEDEFY GKSEIYRDRL TLPVTINQAS AGATLTVTYQ
     GCADAGFCYP PETKTVPLSE VVANNAASQP VSVSQQEQHT AQLPFSALWA LLIGIGIAFT
     PCVLPMYPLI SGIVLGGKQR LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ
     HPYVLIGLAI VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FVMGAIAGLI
     CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL LPKSGPWMEQ
     VKTAFGFVIL ALPVFLLERV IGDVWGLRLW SALGVAFFGW AFITSLQAKR GWMRVVQIIL
     LAAALVSVRP LQDWAFGATH TAQTQTHLNF TQIKTVDELN HALVEAKGKP VMLDLYADWC
     VACKEFEKYT FSDPQVQKAL ADTVLLQANI TANDAQDVAL LKHLNVLGLP TILFFDGQGQ
     EHPQARVTGF MDAETFSAHL RDRQP