(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILE0_PSEHT

ID   Q3ILE0_PSEHT            Unreviewed;       233 AA.
AC   Q3ILE0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 75.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbC {ECO:0000313|EMBL:CAI85605.1};
GN   OrderedLocusNames=PSHAa0515 {ECO:0000313|EMBL:CAI85605.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85605.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85605.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85605.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3ILE0; -.
DR   STRING; 326442.PSHAa0515; -.
DR   EnsemblBacteria; CAI85605; CAI85605; PSHAa0515.
DR   KEGG; pha:PSHAa0515; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222077; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; POG091H04JN; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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;
DR   PRODOM; Q3ILE0.
DR   SWISS-2DPAGE; Q3ILE0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Isomerase {ECO:0000313|EMBL:CAI85605.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   DOMAIN       30     75       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      103    227       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   233 AA;  24647 MW;  6A88C1D2DAA13C8A CRC64;
     MLCTSLSAVA NDVAVAPNAN DPIVIKFAAL GVTVKQINPS PVAGLKELIT NQGVLYASPD
     GQFLMQGTLI DLNNRSNLTE KALNGVRQAG LKEYEDSMIV YKAPNEKHSI TVFTDISCGY
     CRKLHRELDD LLEAGITVKY LAFPRGGLQG SGYNDLMNVW CAKDQQEALT EAKSGSNTTA
     VKGCSAPVAE HYQLGQSFGV TGTPAIILED GTMIPGYQPA AALSAALNAS KAP
//

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