GenomeNet

Database: UniProt
Entry: H8YL93_AERHY
LinkDB: H8YL93_AERHY
Original site: H8YL93_AERHY 
ID   H8YL93_AERHY            Unreviewed;       213 AA.
AC   H8YL93;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
OS   Aeromonas hydrophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644 {ECO:0000313|EMBL:AFD54047.1};
RN   [1] {ECO:0000313|EMBL:AFD54047.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AH-3 {ECO:0000313|EMBL:AFD54047.1};
RX   PubMed=22198000; DOI=10.1016/j.micpath.2011.10.006;
RA   Vilches S., Jimenez N., Merino S., Tomas J.M.;
RT   "The Aeromonas dsbA mutation decreased their virulence by triggering type
RT   III secretion system but not flagella production.";
RL   Microb. Pathog. 52:130-139(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF747155; AFD54047.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8YL93; -.
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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..213
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003617496"
FT   DOMAIN          19..160
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        61..64
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   213 AA;  23831 MW;  F8C0DB2317B2CA87 CRC64;
     MPHSDPLTGN VMKKVLFFLA AMLMIPMVHA APEFKEGVNY DVVKQTGSAQ PEVLEFFSYY
     CPHCAKFEPI AADLKKNLPE GVPMKKNPVA FLGREMGPEM QRAYAVASLL NVEGKLTPAI
     FDKIHTQRQY PQSRTDVKQI FVDNGVPAEE FDGAVDSFAV SGMVSQFDRN TESYNIRGVP
     AFLVNGKYMV KIESITSQEQ FNQLVKFLLA KKD
//
DBGET integrated database retrieval system