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Database: UniProt
Entry: A0A0K1XEL8_9GAMM
LinkDB: A0A0K1XEL8_9GAMM
Original site: A0A0K1XEL8_9GAMM 
ID   A0A0K1XEL8_9GAMM        Unreviewed;       214 AA.
AC   A0A0K1XEL8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   ORFNames=AKN88_06985 {ECO:0000313|EMBL:AKX59699.1};
OS   Thiopseudomonas alkaliphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Thiopseudomonas.
OX   NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59699.1, ECO:0000313|Proteomes:UP000063953};
RN   [1] {ECO:0000313|EMBL:AKX59699.1, ECO:0000313|Proteomes:UP000063953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E5571 {ECO:0000313|EMBL:AKX59699.1,
RC   ECO:0000313|Proteomes:UP000063953};
RX   PubMed=26679585;
RA   Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA   Juieng P., Loparev V., McQuiston J.R.;
RT   "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT   a Novel Bacterium of the Pseudomonadaceae Family.";
RL   Genome Announc. 3:e01474-15(2015).
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; CP012365; AKX59699.1; -; Genomic_DNA.
DR   RefSeq; WP_053100871.1; NZ_JACANE010000005.1.
DR   AlphaFoldDB; A0A0K1XEL8; -.
DR   STRING; 1697053.AKN87_09405; -.
DR   GeneID; 82260684; -.
DR   PATRIC; fig|1697052.3.peg.1476; -.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000063953; Chromosome.
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; 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   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063953};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..214
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005472116"
FT   DOMAIN          14..166
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   214 AA;  23933 MW;  A0CDF68DEC381C7F CRC64;
     MRKLLLSSFL ATSCLFGAQA LAVEPVAGTN YVVLESPVAV SKKDQIEVVE LFWYGCPHCY
     QLEPTLNPWV EQLPEDVNFV KMPAMFGGAW DVHGQLFYTL QALKVEQKVH DRVFDALHNK
     KQRLANAKEI ASFLEADGID QDTFNKTWNS FGVKSQMEKA RQQAMAYQVQ GVPALVINGK
     YRFDIGMAGG LTETTELADA LIAQERQATE SEQE
//
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