ID V8G301_9BURK Unreviewed; 206 AA.
AC V8G301;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=V757_08405 {ECO:0000313|EMBL:ETD70037.1};
OS Pelistega indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pelistega.
OX NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD70037.1, ECO:0000313|Proteomes:UP000018766};
RN [1] {ECO:0000313|EMBL:ETD70037.1, ECO:0000313|Proteomes:UP000018766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM-7 {ECO:0000313|EMBL:ETD70037.1,
RC ECO:0000313|Proteomes:UP000018766};
RA Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT "Genomic analysis of Pelistega sp. HM-7.";
RL Submitted (NOV-2013) 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:ETD70037.1}.
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DR EMBL; AYSV01000091; ETD70037.1; -; Genomic_DNA.
DR RefSeq; WP_023951656.1; NZ_CABMIG010000091.1.
DR AlphaFoldDB; V8G301; -.
DR PATRIC; fig|1414851.3.peg.1735; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000018766; 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:UP000018766};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..206
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004769214"
FT DOMAIN 7..152
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 206 AA; 23025 MW; 1E6DE363D9528A0A CRC64;
MLTLKTLKTL IPALGFVALS TFSTAQAQEK YITFNPAFAS QTPAKTEVLE FFSYACSHCA
AMEPMVENLS KELPASAELL PVPVAFNASM EPMQRLFYTL MALDRKDLHP KVFEAIHKDK
KRLFTRDVIV DWAVSQGIDK KTFEETYDSF GVNTKVRRAT EMTDQYKVDA TPSFAVAGKY
LTSPGMTGDY ESAIVLVKQL VEKEAK
//
