ID G3A3V9_9RALS Unreviewed; 218 AA.
AC G3A3V9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN Name=dsbA {ECO:0000313|EMBL:CCA88570.1};
GN ORFNames=RALSY_30318 {ECO:0000313|EMBL:CCA88570.1};
OS Ralstonia syzygii R24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA88570.1};
RN [1] {ECO:0000313|EMBL:CCA88570.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA88570.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA88570.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA88570.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) 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; FR854088; CCA88570.1; -; Genomic_DNA.
DR AlphaFoldDB; G3A3V9; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:CCA88570.1};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..218
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003442106"
FT DOMAIN 15..211
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 218 AA; 24062 MW; 219A8F34B3F6BEE5 CRC64;
MKKLAAFLIV LATGAGFLMT APAQAAPTAG KEYKVLPTPQ PVPTGKVEVT EFFWYGCPHC
YDFENTWTAW AAKQGKDVVI KRVPVAFNPK LEPHTRIYYT LEALGKLDAK DASGRTLHDR
VFDQLHKNYR SMSEPDQIAD FMAANGVDRK AFLDAYNSFG VNANTKRAAQ LADQYKIEGV
PTVVVQGKYT TSPADAGSNV GTAQTLDYLV QQVRDHKM
//
