ID A0A0H3KHT3_BURM1 Unreviewed; 212 AA.
AC A0A0H3KHT3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN Name=dsbA {ECO:0000313|EMBL:BAG44759.1};
GN OrderedLocusNames=BMULJ_02871 {ECO:0000313|EMBL:BAG44759.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG44759.1, ECO:0000313|Proteomes:UP000008815};
RN [1] {ECO:0000313|EMBL:BAG44759.1, ECO:0000313|Proteomes:UP000008815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|PIRNR:PIRNR001488}.
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DR EMBL; AP009385; BAG44759.1; -; Genomic_DNA.
DR RefSeq; WP_006398112.1; NC_010804.1.
DR AlphaFoldDB; A0A0H3KHT3; -.
DR STRING; 395019.BMULJ_02871; -.
DR GeneID; 66527805; -.
DR KEGG; bmj:BMULJ_02871; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_1_0_4; -.
DR Proteomes; UP000008815; Chromosome 1.
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; IPR023205; DsbA/DsbL.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; PF13462; Thioredoxin_4; 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|PIRNR:PIRNR001488};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000008815};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..212
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002613468"
FT DOMAIN 10..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 212 AA; 23277 MW; 390331CF78980E7D CRC64;
MKKLLSTLLL SLGLAAGFAQ ASPAAPVAGK DFEVMKSPQP VSAPAGKVEV IEFFWYGCPH
CYEFEPTIEA WVKKQGGNIE FKRVPVAFRD DFVPHSRLYY AVSALGIAEK VTPAIFNAIH
KQKNYLLTPQ AQADFLATQG VDKKQFMDAY NSFSVQGQVK QSAELLKNYA IDGVPTIVVQ
GKYKTGPAYT NSIPGTAQVL DFLVKQVQDK KL
//
