ID   A0A011QGU7_9PROT        Unreviewed;       608 AA.
AC   A0A011QGU7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   12-AUG-2020, entry version 28.
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; Candidatus Accumulibacter;
OC   unclassified 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 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI88517.1}.
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DR   EMBL; JEMY01000026; EXI88517.1; -; Genomic_DNA.
DR   STRING; 1454004.AW11_02137; -.
DR   PATRIC; fig|1454004.3.peg.2214; -.
DR   eggNOG; COG4232; Bacteria.
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   Gene3D; 3.40.30.10; -; 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|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, ECO:0000313|EMBL:EXI88517.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_00399}; Reference proteome {ECO:0000313|Proteomes:UP000022141};
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   TRANSMEM        191..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        238..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        273..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        317..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        359..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        395..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        448..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DOMAIN          467..608
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        138..144
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        524..527
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//