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Database: UniProt
Entry: K0MFU8_BORPB
LinkDB: K0MFU8_BORPB
Original site: K0MFU8_BORPB 
ID   K0MFU8_BORPB            Unreviewed;       231 AA.
AC   K0MFU8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Probable glutathione S-transferase {ECO:0000313|EMBL:CCJ49674.1};
GN   OrderedLocusNames=BN117_2341 {ECO:0000313|EMBL:CCJ49674.1};
OS   Bordetella parapertussis (strain Bpp5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ49674.1, ECO:0000313|Proteomes:UP000008035};
RN   [1] {ECO:0000313|EMBL:CCJ49674.1, ECO:0000313|Proteomes:UP000008035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ49674.1,
RC   ECO:0000313|Proteomes:UP000008035};
RX   PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA   Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA   Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT   "Comparative genomics of the classical Bordetella subspecies: the evolution
RT   and exchange of virulence-associated diversity amongst closely related
RT   pathogens.";
RL   BMC Genomics 13:545-545(2012).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; HE965803; CCJ49674.1; -; Genomic_DNA.
DR   RefSeq; WP_003812170.1; NC_018828.1.
DR   RefSeq; YP_006896253.1; NC_018828.1.
DR   AlphaFoldDB; K0MFU8; -.
DR   GeneID; 69420739; -.
DR   KEGG; bpar:BN117_2341; -.
DR   HOGENOM; CLU_011226_14_4_4; -.
DR   Proteomes; UP000008035; Chromosome.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..215
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          205..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  25818 MW;  C98BA7942A4F4894 CRC64;
     MIDLYFWATP NGLKIKLFLE EAGLPYTEHP INIGKGEQFQ REFLAIAPNN RIPAIVDQAP
     AGGGAPISLF ESGAILLYLA EKIGRFIPAD VRGRAEVLQW LFWQMGGLGP MAGQNGHFNV
     YAPEKVPYAI ERYTAETARL YDVMDRRLAE REFLAGEYSI ADIACYPWVV PHEAHGQKMA
     HFPHLSRWFE AIAARPATAR AYKEAGDSYR PKAPMSDEER AVLFGQPGAP R
//
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