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Database: UniProt
Entry: K7YMK8_BDEBC
LinkDB: K7YMK8_BDEBC
Original site: K7YMK8_BDEBC 
ID   K7YMK8_BDEBC            Unreviewed;       557 AA.
AC   K7YMK8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Putative disulfide-isomerase {ECO:0000313|EMBL:AFY01016.1};
GN   ORFNames=Bdt_1317 {ECO:0000313|EMBL:AFY01016.1};
OS   Bdellovibrio bacteriovorus str. Tiberius.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY01016.1, ECO:0000313|Proteomes:UP000010074};
RN   [1] {ECO:0000313|EMBL:AFY01016.1, ECO:0000313|Proteomes:UP000010074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tiberius {ECO:0000313|EMBL:AFY01016.1,
RC   ECO:0000313|Proteomes:UP000010074};
RX   PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA   Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA   Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA   Sockett R.E.;
RT   "Genome analysis of a simultaneously predatory and prey-independent, novel
RT   Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT   predictions of both ancient and recent lateral gene transfer from diverse
RT   bacteria.";
RL   BMC Genomics 13:670-670(2012).
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DR   EMBL; CP002930; AFY01016.1; -; Genomic_DNA.
DR   RefSeq; WP_015090478.1; NC_019567.1.
DR   AlphaFoldDB; K7YMK8; -.
DR   STRING; 1069642.Bdt_1317; -.
DR   KEGG; bbat:Bdt_1317; -.
DR   PATRIC; fig|1069642.3.peg.1301; -.
DR   HOGENOM; CLU_498453_0_0_7; -.
DR   Proteomes; UP000010074; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF13899; Thioredoxin_7; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000313|EMBL:AFY01016.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..557
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003913671"
FT   DOMAIN          121..252
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   COILED          512..557
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   557 AA;  62350 MW;  EF88B4F57AA648AF CRC64;
     MKVLGFILTL LIAASAFGRL SDGKATFTVK DGKIVGAIQK GFHFNREAPA AFAMKGVEIA
     PLVKEESQLV FAMPTKENEA FELGFYVCDD KKTVCEEQRI TYVISGGKLK PASEVKKAEV
     AKPEVKATAG KVHKNSHGFI ENDLEAAKTL AAKLKKNLLV DYGAPWCPAC VRLETEVFGT
     KAFKNVTKDF VLVALNADMS VNKPFGKQYN IKAIPTVLIL KPDGTELYRA LDFAPADVYA
     KRIKDAKKNL QSAADLEKLA QAGDQKAIEA LAVSAYNALD METSVKWYRQ IDSKSDRFAS
     AETQLASQQA RADKKSDEYL AILKKWADLK PQSFTSVTAT NEWAELLKSE KKDLPADLKE
     RLKANTEFLQ NLTKSKADTI KWVEAWDVSP MAPVERAEAL SMWKASAEAL GQKEEIVKIQ
     QELQDEVRSL KLSEKRPGEV MATLFYFRQA GLPEIEESWL LKLEKENPDS YVPHMKLASY
     YVRNKAYDKA LPQAQLAVEL GEDLRLHNLK TLAEIQKELK QKDEAKKTIE IALAHPQVKE
     DRFKEVLKSL EQMKKDL
//
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