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Database: UniProt
Entry: H2G0Y7_OCESG
LinkDB: H2G0Y7_OCESG
Original site: H2G0Y7_OCESG 
ID   H2G0Y7_OCESG            Unreviewed;       200 AA.
AC   H2G0Y7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=GU3_02345 {ECO:0000313|EMBL:AEY00226.1};
OS   Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Oceanimonas.
OX   NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00226.1, ECO:0000313|Proteomes:UP000007742};
RN   [1] {ECO:0000313|EMBL:AEY00226.1, ECO:0000313|Proteomes:UP000007742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GK1 {ECO:0000313|EMBL:AEY00226.1,
RC   ECO:0000313|Proteomes:UP000007742};
RX   PubMed=22461556; DOI=10.1128/JB.00023-12;
RA   Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA   Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT   "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT   from Gavkhouni Wetland in Iran.";
RL   J. Bacteriol. 194:2123-2124(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}.
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DR   EMBL; CP003171; AEY00226.1; -; Genomic_DNA.
DR   RefSeq; WP_014290962.1; NC_016745.1.
DR   AlphaFoldDB; H2G0Y7; -.
DR   STRING; 511062.GU3_02345; -.
DR   KEGG; oce:GU3_02345; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000007742; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000007742};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..200
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003561926"
FT   DOMAIN          10..160
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        50..53
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   200 AA;  22487 MW;  769988CDD9AA77AD CRC64;
     MKTLIFAFVT MLLVPLAQAA SEFQEGVEYT VVAEVPSSKP EVTEFFSYVC PHCYSFEPLM
     DKLAERLPEA DINKVPVAFL GRDMGPVLQR AYGAALLLKV EDKLTPVMFD RIHRQKKMPA
     SLEDVKEVFV ANGVDAKDFD GVINSFALNG MIAKYDKLTE KYNVRGTPTV IVRGKYQLNM
     GEIGSEERFY RVVEYLLSAN
//
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