ID   A0A1H9EKE8_9GAMM        Unreviewed;       218 AA.
AC   A0A1H9EKE8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   ORFNames=SAMN04488038_10569 {ECO:0000313|EMBL:SEQ26095.1};
OS   Solimonas aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Solimonas.
OX   NCBI_TaxID=489703 {ECO:0000313|EMBL:SEQ26095.1, ECO:0000313|Proteomes:UP000199233};
RN   [1] {ECO:0000313|EMBL:SEQ26095.1, ECO:0000313|Proteomes:UP000199233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25927 {ECO:0000313|EMBL:SEQ26095.1,
RC   ECO:0000313|Proteomes:UP000199233};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOFS01000005; SEQ26095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9EKE8; -.
DR   STRING; 489703.SAMN04488038_10569; -.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000199233; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199233};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..218
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011738048"
FT   DOMAIN          11..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        59..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   218 AA;  24049 MW;  36B2683509151412 CRC64;
     MRPLLRGLLA VVLSVSAAAC SAKDSAGFEE GKQYKKVMAV QPPSDPKRIS VEEFFWYGCP
     HCYAFDPDIN KWLKTKPADV DFIRVPNSLG HPQGLLHSKA FYTAEALQLY PQLHTVLFDA
     IHKDNLPMNT QEQIGQVFAK AGGVKPDVFA GTFNSFVVEA QVNKAEQLAR TYGVISVPTI
     IVGGKYMTSV QMAGGHDQTL TVINQLVDKI RQERGLKK
//