ID   B3ECV3_CHLL2            Unreviewed;       625 AA.
AC   B3ECV3;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   19-FEB-2014, entry version 47.
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=Clim_1312;
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T.,
RA   Liu Z., Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) 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.
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DR   EMBL; CP001097; ACD90378.1; -; Genomic_DNA.
DR   RefSeq; YP_001943357.1; NC_010803.1.
DR   ProteinModelPortal; B3ECV3; -.
DR   STRING; 290315.Clim_1312; -.
DR   EnsemblBacteria; ACD90378; ACD90378; Clim_1312.
DR   GeneID; 6354505; -.
DR   KEGG; cli:Clim_1312; -.
DR   PATRIC; 21374727; VBIChlLim118737_1401.
DR   eggNOG; COG4232; -.
DR   HOGENOM; HOG000254982; -.
DR   KO; K04084; -.
DR   OMA; YISQTRD; -.
DR   OrthoDB; EOG69D3B9; -.
DR   ProtClustDB; CLSK637588; -.
DR   BioCyc; CLIM290315:GHUH-1343-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; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     31       Potential.
FT   SIGNAL        1     27       By similarity.
FT   CHAIN        32    625       Potential.
FT                                /FTId=PRO_5000374805.
FT   TRANSMEM    207    227       Helical; (By similarity).
FT   TRANSMEM    247    267       Helical; (By similarity).
FT   TRANSMEM    283    303       Helical; (By similarity).
FT   TRANSMEM    327    347       Helical; (By similarity).
FT   TRANSMEM    362    382       Helical; (By similarity).
FT   TRANSMEM    409    429       Helical; (By similarity).
FT   TRANSMEM    430    450       Helical; (By similarity).
FT   TRANSMEM    460    480       Helical; (By similarity).
FT   DOMAIN      476    621       Thioredoxin (By similarity).
FT   DISULFID    131    137       Redox-active (By similarity).
FT   DISULFID    223    344       Redox-active (By similarity).
FT   DISULFID    536    539       Redox-active (By similarity).
SQ   SEQUENCE   625 AA;  66495 MW;  110F31302884C41D CRC64;
     MPVNRNIMLH RTISISGFLL FWLIAFSSNG FGTAFLDPGQ AFRLKAELTS SGSVVLDWAI
     ADGYKLYRDQ VKVSLEKGDA ELRIPGLPAG ESVTDPSTKE RMEVYHDNLR IEVPVVRAAG
     EFTLKVVYQG CAEDGVCYPP FTRTVTIDPA KPGVLNVVED PETGGFGGFA VTEDVPVDSL
     PAAREKKAGD DFSYSQSLLK SRSLLKIGFF FLIFGLALSF TPCILPMIPI LSSIIVGDGC
     YGRGRSFMLA VAYSLGMALV YTLLGVAAGL AGEGLAGALQ QPWVLGMFAL LLVVLALSMF
     DVYQLQIPGI MQSSIAKTCG KLKGGQIAGV FLMGSLSALI VGPCVAAPLA GTLVYISQTR
     HVVIGGLALF SMAMGMSMPL LLVGLSAGTL LPKAGAWMNG VKYLFGLMLI GVAIWMVSPV
     IPGPLALLFW GALAMLCAVF LHLFDSLPEQ SSIAMKFGKA LGIVLLVIGI LELAGAAAGG
     TNPLEPLAPF GSGAGGRTSA EEAGLKFTRI RSYAELDAAL ASAEKPVMLD FYADWCVSCK
     ELEHFTFNDP AVCKQLETMT LLQVDVTANT PDDIALMKRF GIFGPPAIIF FDASGNEIPG
     SRVVGFVEAK PFLDHLDLYL TRNLP
//