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Database: UniProt
Entry: A3YAT6_9GAMM
LinkDB: A3YAT6_9GAMM
Original site: A3YAT6_9GAMM 
ID   A3YAT6_9GAMM            Unreviewed;       208 AA.
AC   A3YAT6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   ORFNames=MED121_09178 {ECO:0000313|EMBL:EAQ65726.1};
OS   Marinomonas sp. MED121.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ65726.1, ECO:0000313|Proteomes:UP000003436};
RN   [1] {ECO:0000313|EMBL:EAQ65726.1, ECO:0000313|Proteomes:UP000003436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED121 {ECO:0000313|EMBL:EAQ65726.1,
RC   ECO:0000313|Proteomes:UP000003436};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) 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}.
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:EAQ65726.1}.
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DR   EMBL; AANE01000005; EAQ65726.1; -; Genomic_DNA.
DR   RefSeq; WP_009834140.1; NZ_CH672431.1.
DR   AlphaFoldDB; A3YAT6; -.
DR   STRING; 314277.MED121_09178; -.
DR   HOGENOM; CLU_088255_1_0_6; -.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000003436; Unassembled WGS sequence.
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..208
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002664524"
FT   DOMAIN          10..189
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        54..57
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   208 AA;  23230 MW;  7EF86546B946A31B CRC64;
     MKKILITLAV LLCLPASLFA ASYSPGNGYT LIKNPVRTAN PEKIEVVEIF WYGCPHCFSL
     EPVTHAWSKN IADDVDFKFM PAVFGRSWQA HAKAFYVSEL LGLQEKTHGA IFNAIHLDKR
     RLNSEDKLAE FFTQYGVSEA NFKKQFNSFA VNSRLSQADS KIRAYGARGV PGLIVNGKYL
     VTAQSAGGNN QIYSVVDFLI EQERQAMK
//
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