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Database: UniProt
Entry: Q3SGG6_THIDA
LinkDB: Q3SGG6_THIDA
Original site: Q3SGG6_THIDA 
ID   Q3SGG6_THIDA            Unreviewed;       236 AA.
AC   Q3SGG6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   25-APR-2018, entry version 77.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=Tbd_2331 {ECO:0000313|EMBL:AAZ98284.1};
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ98284.1, ECO:0000313|Proteomes:UP000008291};
RN   [1] {ECO:0000313|EMBL:AAZ98284.1, ECO:0000313|Proteomes:UP000008291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ98284.1,
RC   ECO:0000313|Proteomes:UP000008291};
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; CP000116; AAZ98284.1; -; Genomic_DNA.
DR   RefSeq; WP_011312843.1; NC_007404.1.
DR   ProteinModelPortal; Q3SGG6; -.
DR   STRING; 292415.Tbd_2331; -.
DR   EnsemblBacteria; AAZ98284; AAZ98284; Tbd_2331.
DR   KEGG; tbd:Tbd_2331; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222078; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; TDEN292415:G1G56-2358-MONOMER; -.
DR   Proteomes; UP000008291; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008291};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008291};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     20       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        21    236       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010003612.
FT   DOMAIN       26     79       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      107    231       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   236 AA;  25781 MW;  CF82ACDD33AB6699 CRC64;
     MKFTSLALAA SLMFAAAAHA DEKLIRKTLA QQFPGAKVSS VKPTPYSGLF EVYLDGQLVY
     VDAKAKYVFA GDVIDLKNRT NLTQARLNQL QAVSWDVFPL NNALKTVKGN GARKLVLFSD
     VDCPYCRKFE AELTKVDNIT VYTFLYPIAG LHPKAVQTSK QIWCAPDRNK AWDAYITRGT
     VPDNDGKCAN PVDATIALGN RLKVNGTPTL FFANGVRVPG MVPAAQLERL LAANAK
//
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