ID   A0A7R6PFH7_9GAMM        Unreviewed;       743 AA.
AC   A0A7R6PFH7;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399};
DE            EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399};
DE   AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE            Short=Disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE   Flags: Precursor;
GN   Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399,
GN   ECO:0000313|EMBL:BBB23360.1};
GN   ORFNames=CVPH_1541 {ECO:0000313|EMBL:BBB23360.1};
OS   Abyssogena phaseoliformis symbiont OG214.
OC   Bacteria; Proteobacteria; Gammaproteobacteria.
OX   NCBI_TaxID=1235283 {ECO:0000313|EMBL:BBB23360.1, ECO:0000313|Proteomes:UP000595698};
RN   [1] {ECO:0000313|EMBL:BBB23360.1, ECO:0000313|Proteomes:UP000595698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OG214 {ECO:0000313|EMBL:BBB23360.1};
RA   Takaki Y., Shimamura S., Nagai Y., Tsuda M., Yoshida T., Maruyama T.;
RT   "Genome analysis of deep-sea clam Calyptogena phaseoliformis
RT   endosymbiont.";
RL   Submitted (DEC-2012) 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:0000256|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:0000256|ARBA:ARBA00000696, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00001346, ECO:0000256|HAMAP-
CC         Rule:MF_00399};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|HAMAP-Rule:MF_00399};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC       ECO:0000256|HAMAP-Rule:MF_00399}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000256|ARBA:ARBA00007241, ECO:0000256|HAMAP-Rule:MF_00399}.
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DR   EMBL; AP012977; BBB23360.1; -; Genomic_DNA.
DR   KEGG; aphf:CVPH_1541; -.
DR   Proteomes; UP000595698; 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; -; 2.
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; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF0; PTHR32234:SF0; 2.
DR   Pfam; PF11412; DsbC; 2.
DR   Pfam; PF02683; DsbD; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF74863; SSF74863; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748,
KW   ECO:0000256|HAMAP-Rule:MF_00399};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00399};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00399};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00399};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00399};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00399}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   CHAIN           21..743
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT                   /id="PRO_5033183281"
FT   TRANSMEM        326..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        370..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        447..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        486..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        522..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        549..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        579..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DOMAIN          608..743
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        118..124
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        345..467
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        658..661
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   743 AA;  81337 MW;  F18589B776C9727D CRC64;
     MKRLLLPLFL LLSAFSLVQV EDDLLPVDKA FVFKASVVNN EILLNWDIAK GYYLYKEKIK
     ISADFSAQLG NAKFPTAKIR NDEFFGKIGV YRDNAVVVVP VLKGDTESIL LTVSYQGCAD
     LGVCYPPITK SVALSIGSMR STSLTDNVFN LFSRVTNKAQ SIVEKIIPIS DEPLPADDAF
     KFSVVAIDAN TLLVKWTIHQ EYYLYHDKFF FDIKGAKFGD IVFPKGKIKD DEFFGKIEVH
     KGVLEVKIPL INVSNQPITF IVKYQGCWEG GVCYPPQEKT KDITLLSQVD DSNINTAPEK
     PQAPSIEQVE LNETDQITAL LQQDNILLVL ASFFGFGLLL SLTPCVFPMI PILSGIIVGQ
     KGEVSTKKAL IMSIVFVLSM SITYSIAGVL AGYFGENLQV LFQTPWILAI FSLIFVALAF
     SMFGYYEIQL PANLQGKITK ISNGQEGGHL IGVAIMGFLS ALIVGPCVAP PLAGALIYIG
     QTGDTLLGGL SLFVMSLGMG APLVAIGAGI SKLPKAGGWM DNIKYVFGIL MLAVAIYLLD
     RIISPLTSLV LWAMLTTISP IAMGALSTQT STSSPWQRIF KALGLIILGY GILLWILVAR
     GGGDMFQPLS GWGASSITTE SVHIKFERVK SVNELDQILA KAKSNNQIVM LDFYADWCIS
     CKELERFVFS NASVVNEMAM ANVIALQADV TENNANDKAL MKRFGLVGPP AILFFNNDIE
     NRSQRIIGEI NAQDFLSHLN KTK
//