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Database: UniProt
Entry: B1XSF2_POLNS
LinkDB: B1XSF2_POLNS
Original site: B1XSF2_POLNS 
ID   B1XSF2_POLNS            Unreviewed;       215 AA.
AC   B1XSF2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=Pnec_1684 {ECO:0000313|EMBL:ACB44751.1};
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB44751.1};
RN   [1] {ECO:0000313|EMBL:ACB44751.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1 {ECO:0000313|EMBL:ACB44751.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT   "Complete sequence of Polynucleobacter necessarius STIR1.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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DR   EMBL; CP001010; ACB44751.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1XSF2; -.
DR   STRING; 452638.Pnec_1684; -.
DR   KEGG; pne:Pnec_1684; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_1_0_4; -.
DR   OrthoDB; 9784896at2; -.
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; IPR017937; Thioredoxin_CS.
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.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..215
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002773094"
FT   DOMAIN          51..185
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   DISULFID        59..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   215 AA;  24421 MW;  262C08E7AF4BBE2D CRC64;
     MISFSKRAIT LLALLFLSGF ASAQTQKIEE GFDYRILPIA QPVEAKGKVE VIEFFLYGCP
     HCYDFGPELS GWVKRQPKDV VFKRVPVAFR DDLMPHSQLF YALEAMGKGD ALNEKVMYAM
     HKENKRLLTE SEIADWVASQ EIDRNTFLAT YRSFAVISKA RAAKQMAEAY RIDGVPTIVM
     QGKYVTSPSI AGSKTKAIVV MDYLEQKIRK DKYKQ
//
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