(data stored in SCRATCH zone)

SWISSPROT: A8FPS4_SHESH

ID   A8FPS4_SHESH            Unreviewed;       202 AA.
AC   A8FPS4;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=Ssed_0234 {ECO:0000313|EMBL:ABV34847.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34847.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34847.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34847.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR001488}.
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DR   EMBL; CP000821; ABV34847.1; -; Genomic_DNA.
DR   RefSeq; WP_012004373.1; NC_009831.1.
DR   ProteinModelPortal; A8FPS4; -.
DR   STRING; 425104.Ssed_0234; -.
DR   EnsemblBacteria; ABV34847; ABV34847; Ssed_0234.
DR   KEGG; sse:Ssed_0234; -.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265317; -.
DR   KO; K03673; -.
DR   OMA; YEVAKIQ; -.
DR   OrthoDB; POG091H040A; -.
DR   BioCyc; SSED425104:GH7Q-237-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPS4.
DR   SWISS-2DPAGE; A8FPS4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    202       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002722139.
FT   DOMAIN       36    190       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13462}.
FT   DISULFID     49     52       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR001488-1}.
SQ   SEQUENCE   202 AA;  22036 MW;  D967F7EDEA7B030B CRC64;
     MIKLLSTAAI LLSFGASAAS FTQGEHYVDL GEAAFNAPNQ VTKVYSVNCP FCYKYEKAVI
     PGFVKNLPDG VSFDSYHITT KPPFGKEKAT VIAVAKVLGD KQYKTAKMAY YKHIHDDKKK
     FSSAEDAISF GLKAAKIDSV TFSAHKDTSE VKALLTQWDQ GVAVAKVRGI PAIVVNGKYL
     INTKTITSMT MLDELTAELL EK
//

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