ID A0A0P7DEF1_9GAMM Unreviewed; 214 AA.
AC A0A0P7DEF1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=AOG28_11000 {ECO:0000313|EMBL:KPM78362.1};
OS Cobetia sp. UCD-24C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Cobetia.
OX NCBI_TaxID=1716176 {ECO:0000313|EMBL:KPM78362.1, ECO:0000313|Proteomes:UP000050261};
RN [1] {ECO:0000313|EMBL:KPM78362.1, ECO:0000313|Proteomes:UP000050261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-24C {ECO:0000313|EMBL:KPM78362.1,
RC ECO:0000313|Proteomes:UP000050261};
RA Krusor M., Coil D.A., Lang J.M., Eisen J.A., Alexiev A.;
RT "Draft Genome of Cobetia sp. UCD-24C.";
RL Submitted (SEP-2015) 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:KPM78362.1}.
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DR EMBL; LJTD01000006; KPM78362.1; -; Genomic_DNA.
DR RefSeq; WP_043333328.1; NZ_LJTD01000006.1.
DR AlphaFoldDB; A0A0P7DEF1; -.
DR STRING; 1716176.AOG28_11000; -.
DR PATRIC; fig|1716176.3.peg.2988; -.
DR Proteomes; UP000050261; 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; 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:UP000050261};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..214
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006137800"
FT DOMAIN 11..201
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 214 AA; 23647 MW; 1947D414463D16A1 CRC64;
MKWKPLLTLV AGLGLSASVF AAEAGKDYQV LDEPVKTDAP AGNVEVVEAF WYGCPHCYKL
ESSLEPWVDE LPSDVTFNRL PATMGQDWVK HAYAFYAAKD LGILDETHKA FFDAIHQDHQ
RLTDPDDIAK FYSDYGVSEE DAKKSLTSFG VKSQVNQAHA QMRAYKIMGV PALIVDGRYV
ISPSTAGSLQ NMLKITDELV EQVREEKAGS KDAA
//
