ID A0A068R9K0_9GAMM Unreviewed; 207 AA.
AC A0A068R9K0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN Name=dsbA {ECO:0000313|EMBL:CDG22840.1};
GN ORFNames=XPG1_3204 {ECO:0000313|EMBL:CDG22840.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG22840.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG22840.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG22840.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; FO704551; CDG22840.1; -; Genomic_DNA.
DR RefSeq; WP_045959684.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068R9K0; -.
DR STRING; 1354304.XPG1_3204; -.
DR KEGG; xpo:XPG1_3204; -.
DR HOGENOM; CLU_088255_3_0_6; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000032735; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
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; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..207
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001654670"
FT DOMAIN 6..149
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 49..52
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 207 AA; 23138 MW; B98BBE67FFBF3631 CRC64;
MKKFWLALMG ALMAFNVCAA GFSEGKQYTE LSKPVADMPQ VLEFFSFYCP HCYQFENVYH
VPSTIRKNLP EGVKIERYHV DFLGNLGEAL TNSWAVAIVM KIEDKVTPIL FEGIQKSQTI
NSEKDIRDAF IKAGVSGEEY DAALNSFIVK SIAAKERQAA KNLNLRGVPA VFVGGNYLVN
NSGIDTNSEL DYAQKFSEVV NYLVNKK
//
