ID   Q8KDH5_CHLTE            Unreviewed;       607 AA.
AC   Q8KDH5;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   19-FEB-2014, entry version 85.
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; OrderedLocusNames=CT1075;
OS   Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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.
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DR   EMBL; AE006470; AAM72308.1; -; Genomic_DNA.
DR   RefSeq; NP_661966.1; NC_002932.3.
DR   ProteinModelPortal; Q8KDH5; -.
DR   SMR; Q8KDH5; 488-607.
DR   STRING; 194439.CT1075; -.
DR   EnsemblBacteria; AAM72308; AAM72308; CT1075.
DR   GeneID; 1006939; -.
DR   KEGG; cte:CT1075; -.
DR   PATRIC; 21400141; VBIChlTep116050_0982.
DR   HOGENOM; HOG000254982; -.
DR   KO; K04084; -.
DR   OMA; YISQTRD; -.
DR   OrthoDB; EOG69D3B9; -.
DR   ProtClustDB; CLSK637588; -.
DR   BioCyc; CTEP194439:GHN0-1112-MONOMER; -.
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; Complete proteome;
KW   Cytochrome c-type biogenesis; Disulfide bond; Electron transport;
KW   Membrane; NAD; Oxidoreductase; Redox-active center;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     11       By similarity.
FT   TRANSMEM    195    215       Helical; (By similarity).
FT   TRANSMEM    231    251       Helical; (By similarity).
FT   TRANSMEM    267    287       Helical; (By similarity).
FT   TRANSMEM    311    331       Helical; (By similarity).
FT   TRANSMEM    347    367       Helical; (By similarity).
FT   TRANSMEM    381    401       Helical; (By similarity).
FT   TRANSMEM    409    429       Helical; (By similarity).
FT   TRANSMEM    444    464       Helical; (By similarity).
FT   DISULFID    110    116       Redox-active (By similarity).
FT   DISULFID    207    328       Redox-active (By similarity).
FT   DISULFID    524    527       Redox-active (By similarity).
SQ   SEQUENCE   607 AA;  63812 MW;  984D5F148A662C82 CRC64;
     MLFMRSASAM AADFLDPEQA FVPSAELTAN RSIAVHWKIA KSYKLYRDQI KVGVSGGKAS
     LGEPVFPEGI LFTDPSTGEK QVIYHDELRL EVPVKQASAP FTVKVEYQGC AEDGLCYPPI
     SKSFKVDPSR PGALAAVEST PDTGASTGLQ PAASDAAPAV AASSANAVDN GGKNDLSLAQ
     STLESGSLWK VFAAFLLFGL LLSFTPCVLP MVPILSSIIV GEGETTKAKS FLMALAYCLG
     MALVYTSLGV AAGLAGEGLA GALQKPWVLV MFSLLLIGLS LSMFDVYQLQ APASLQNSLS
     KTSSKLKGGR FVGVFFMGAI SALIVGPCVA APLAGTLVYI SQTKDVVIGG LALFSMAMGM
     SVPLLLIGLS AGSLLPKAGA WMIGVKYVFG LMLIAVAIWM VTPVLPPQAL MVAWGALGIL
     CAVFAGVFGH LPEKLTVGGK FKKALGLVLF IIGVMELAGA ASGGTNPLEP LAGLRGGSSV
     AAANNGKTAE LAFKKIRTVE DLDRELHASA GKKPVMLDFY ADWCVSCKEF EKFTFSNAKV
     QQGLADVTLL QVDVTANTAD DKALMKRFNL FGPPGIIFFD KSGNEQVDNR IVGFVEAEEF
     LKHLEKL
//