ID U1ZP68_9BURK Unreviewed; 213 AA.
AC U1ZP68;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=N879_11250 {ECO:0000313|EMBL:ERI32866.1};
OS Alcaligenes sp. EGD-AK7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERI32866.1, ECO:0000313|Proteomes:UP000016497};
RN [1] {ECO:0000313|EMBL:ERI32866.1, ECO:0000313|Proteomes:UP000016497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERI32866.1};
RX PubMed=24407646;
RA Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA Purohit H.J., Kapley A.;
RT "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT agricultural soil.";
RL Genome Announc. 2:e01149-13(2014).
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:ERI32866.1}.
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DR EMBL; AVOG02000034; ERI32866.1; -; Genomic_DNA.
DR RefSeq; WP_009463582.1; NZ_AVOG02000034.1.
DR AlphaFoldDB; U1ZP68; -.
DR PATRIC; fig|1386079.3.peg.2187; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000016497; 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:UP000016497};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..213
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004622154"
FT DOMAIN 17..205
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 62..65
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 213 AA; 23241 MW; 1BF42F756278E33B CRC64;
MKLNALFVRS LVGASLLAGA TLLPATSALA QQADQGYVTL PAAQPSDSVG KTEVLEFFSY
SCPHCAILEP KVEAWSKTLP DNVVLRRVPV AFNAGMTDLQ KLYYTLEAMD RLDLHPKVFE
AIHQKRERIF DAKTITAWAA AQGVDKARFE QTFNSFGVQT KANKANELSN TYQIQGTPSL
AVGGKFVTSP ALANGYDESI TKAQELVKMV TNR
//
