ID   A0A011QGU7_9PROT        Unreviewed;       608 AA.
AC   A0A011QGU7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   10-APR-2019, entry version 24.
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};
GN   Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399,
GN   ECO:0000313|EMBL:EXI88517.1};
GN   ORFNames=AW11_02137 {ECO:0000313|EMBL:EXI88517.1};
OS   Candidatus Accumulibacter sp. BA-93.
OC   Bacteria; Proteobacteria; Betaproteobacteria;
OC   Candidatus Accumulibacter.
OX   NCBI_TaxID=1454004 {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141};
RN   [1] {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required to facilitate the formation of correct
CC       disulfide bonds in some periplasmic proteins and for the assembly
CC       of the periplasmic c-type cytochromes. Acts by transferring
CC       electrons from cytoplasmic thioredoxin to the periplasm. This
CC       transfer involves a cascade of disulfide bond formation and
CC       reduction steps. {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,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.8.1.8; Evidence={ECO:0000256|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,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.8.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00399};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00399}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EXI88517.1}.
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DR   EMBL; JEMY01000026; EXI88517.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A011QGU7; -.
DR   STRING; 1454004.AW11_02137; -.
DR   PATRIC; fig|1454004.3.peg.2214; -.
DR   Proteomes; UP000022141; Unassembled WGS sequence.
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 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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 {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Complete proteome {ECO:0000313|Proteomes:UP000022141};
KW   Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093715};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000313|EMBL:EXI88517.1};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022141};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00464121};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093729};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   TRANSMEM    191    218       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    238    261       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    273    296       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    317    347       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    359    383       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    395    412       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    448    469       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DOMAIN      467    608       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID    138    144       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    524    527       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
SQ   SEQUENCE   608 AA;  64989 MW;  497E8D24EF2DC87E CRC64;
     MTWLFVLPHS VRRFFQRSSL LPFLLPVLML LTWPAQGEEF LDPAVAFKPT AHAVDGQTIE
     VRFEIAKGYY LYRDKFRFTA EPASVQLGTP ILSPGKVKED PNFGKVEVYY KQALIRIPVE
     RNSSGPLPLT LKITSQGCAD AGICYPPQRQ TLALELPDPA TTPSAGATTP GKDFGDDESG
     RIAQLFGNAS FWLLVASFFG FGLLLSLTPC CFPMIPILSS IIVGSGRDGH GVSHARGFSL
     SLAYVLGMAI TYAAAGVAAG LTGTLLTAAL QNAWVLGAFA LVFVALSLSM FGFYELQLPT
     FLQSKVSEEA SHLRGGSLPG VAAMGVLSAI IVGPCVAAPL AGALLYIGRS GDAVLGGAAL
     FAMGLGMGAP LLAVGLSAGT LLPRSGPWME AVKKSFGVLL LATAVWLLSP VVPVVAQMIA
     WALLLIVPAI YMHALDPLPP HARGWQRFWK GIGIFMLIGG AAMLLGALAG SRDPLQPLSA
     LRSSAAEVEV KQLPFTRVRT LAELERRIKS AGQPVMIDFY ADWCVSCKEM ERFTFADARV
     RAKLAGWTLL QADVTANSDE DKALLQRFNL YGPPGIIFFD AQGREIDGVR VVGFMSADEF
     LGLLARLG
//