ID   A0A011QGU7_9PROT        Unreviewed;       608 AA.
AC   A0A011QGU7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   17-FEB-2016, entry version 9.
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   Flags: Precursor;
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: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H. {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   -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000256|HAMAP-
CC       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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JEMY01000026; EXI88517.1; -; Genomic_DNA.
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 carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-HAMAP.
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; IPR028250; DsbDN.
DR   InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
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   ECO:0000256|SAAS:SAAS00512526};
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:SAAS00464083};
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   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:SAAS00464105};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   SIGNAL        1     37       {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   CHAIN        38    608       Thiol:disulfide interchange protein DsbD.
FT                                {ECO:0000256|HAMAP-Rule:MF_00399}.
FT                                /FTId=PRO_5004993609.
FT   TRANSMEM    185    205       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    242    262       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    273    293       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    327    347       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    354    374       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    388    408       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    411    431       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    451    471       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    210    335       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
//