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Database: UniProt
Entry: G7G590_9GAMM
LinkDB: G7G590_9GAMM
Original site: G7G590_9GAMM 
ID   G7G590_9GAMM            Unreviewed;       212 AA.
AC   G7G590;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   Name=dsbA {ECO:0000313|EMBL:GAA80563.1};
GN   ORFNames=P20495_3078 {ECO:0000313|EMBL:GAA80563.1};
OS   Pseudoalteromonas sp. BSi20495.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA80563.1, ECO:0000313|Proteomes:UP000003050};
RN   [1] {ECO:0000313|Proteomes:UP000003050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX   PubMed=22275105; DOI=10.1128/JB.06427-11;
RA   Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT   ice.";
RL   J. Bacteriol. 194:908-909(2012).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAA80563.1}.
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DR   EMBL; BADY01000114; GAA80563.1; -; Genomic_DNA.
DR   RefSeq; WP_008137604.1; NZ_BADY01000114.1.
DR   AlphaFoldDB; G7G590; -.
DR   Proteomes; UP000003050; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..212
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003494651"
FT   DOMAIN          12..137
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   212 AA;  23832 MW;  6E69B6A45C2152DA CRC64;
     MIKLVKAGLL AVLLPMAAAS FAATYEEGVH YDVVSERATK KPEVKEFFSF YCPACNNMEA
     VIGEFKPKLD KNVKFKKSHV DFVGVRDPEN QQMMSQALAT AEVLPQKDQI ISAIFNHIHT
     KRAKFNELAD VKDIFVAQGV DGDKFDKLFK SFSVRTLSSK MKRDQDYFKE KGALRGVPTF
     IVNGKYKLNL GRESGITEPE DIGKLINYLA NK
//
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