ID   Q0YTJ9_9CHLB            Unreviewed;       620 AA.
AC   Q0YTJ9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   19-FEB-2014, entry version 50.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD;
DE            EC=1.8.1.8;
DE   AltName: Full=Protein-disulfide reductase;
DE   Flags: Precursor;
GN   Name=dsbD; ORFNames=CferDRAFT_1562;
OS   Chlorobium ferrooxidans DSM 13031.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=377431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 13031;
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM
RT   13031.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 13031;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Chlorobium ferroxidans
RT   DSM 13031.";
RL   Submitted (JUL-2006) 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; AASE01000003; EAT59555.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0YTJ9; -.
DR   SMR; Q0YTJ9; 499-617.
DR   EnsemblBacteria; EAT59555; EAT59555; CferDRAFT_1562.
DR   PATRIC; 27056728; VBIChlFer75923_0583.
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; PTHR32234; 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;
KW   Transport.
FT   SIGNAL        1     29       Potential.
FT   SIGNAL        1     28       By similarity.
FT   CHAIN        30    620       Potential.
FT                                /FTId=PRO_5000041629.
FT   TRANSMEM    209    229       Helical; (By similarity).
FT   TRANSMEM    245    265       Helical; (By similarity).
FT   TRANSMEM    281    301       Helical; (By similarity).
FT   TRANSMEM    325    345       Helical; (By similarity).
FT   TRANSMEM    360    380       Helical; (By similarity).
FT   TRANSMEM    401    421       Helical; (By similarity).
FT   TRANSMEM    422    442       Helical; (By similarity).
FT   TRANSMEM    458    478       Helical; (By similarity).
FT   DOMAIN      479    618       Thioredoxin (By similarity).
FT   DISULFID    127    133       Redox-active (By similarity).
FT   DISULFID    221    342       Redox-active (By similarity).
FT   DISULFID    533    536       Redox-active (By similarity).
SQ   SEQUENCE   620 AA;  65860 MW;  47A90CE200037972 CRC64;
     MTHYYFRRAA ALFTFFMVLC STVRVAFAAE FLDPDQAFKL RAELSGSKTI LLNWEIAKGY
     KLYQDKVKAT VDGGAAKLQN PVMPKAILYT DPTTNEKLAI YHDRLSVSAP VVKADGIFTL
     NVEYQGCAED GLCYPPITKS FTVDPSKPGV LAVAGEQPVA DAGSVTPPAD SAAAPSSVAP
     TEVKPADNDL NLAKSTLAGG SLWKIALAFL AFGLLLSFTP CVLPMIPILS SIIVGEGEVT
     RRRSFLMALA YCLGMALVYT SLGVAAGLAG EGLAGALQKP WVLILFALLL VTLSLSMFDV
     YQLQMPASIQ NKLNKTSGNL KGGRFVGVFL MGSLSALIVG PCVAAPLAGT LVYISQTKDV
     VIGGLALFSM AMGMSVPLLL VGLSAGSLLP RAGAWMIGVK YVFGLLLIAV AIWMVSPVIP
     AQAVMIAWGA YTILCAVFLG VFDKHAEKST IAQKFGKALG LVLFIIGVLE LIGATSGGTD
     VLKPLSGFHA SAVSVSGDEK RVAFTQIRSA AELDQALQSA EKPVMLDFYA DWCVACKEMD
     KFTFHDPQVI SQFNNLTLLQ VDVTANSADD RELMKRFGLF GPPGMIFFDA SGKEIPDSRV
     IGFLEAPAFS THLSKFVAGS
//