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
//