ID A0A1E8CLL5_9GAMM Unreviewed; 213 AA.
AC A0A1E8CLL5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=PHACT_09350 {ECO:0000313|EMBL:OFE13318.1};
OS Pseudohongiella acticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1524254 {ECO:0000313|EMBL:OFE13318.1, ECO:0000313|Proteomes:UP000175669};
RN [1] {ECO:0000313|Proteomes:UP000175669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42131 {ECO:0000313|Proteomes:UP000175669};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {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:OFE13318.1}.
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DR EMBL; MASR01000001; OFE13318.1; -; Genomic_DNA.
DR RefSeq; WP_070117275.1; NZ_MASR01000001.1.
DR AlphaFoldDB; A0A1E8CLL5; -.
DR STRING; 1524254.PHACT_09350; -.
DR Proteomes; UP000175669; 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; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
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; PS00862; OX2_COVAL_FAD; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000175669};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..213
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009212161"
FT DOMAIN 97..194
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 213 AA; 23979 MW; E0A3B39799C9AA73 CRC64;
MIKQVVKLGA AALLSALAVS AWAQPSLYVA GTHYEELPAP VRTNDADRIE VLEVFWYGCG
HCFRFQPLVD DWAANAPDDV DYQRYPAIWN ELMKVHAQAY YTAEALDAVE AVHEPIFNAI
NLQGNRLQNE QQLATLFTDH GVDEDAFSRA FNSFPVRTKV NQAESRMQDY QIRSTPNVIV
NGKYLVTTNE AVRTQQDMLS IVDFLVAQER AAL
//
