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Database: UniProt
Entry: A9I9Y6_BORPD
LinkDB: A9I9Y6_BORPD
Original site: A9I9Y6_BORPD 
ID   A9I9Y6_BORPD            Unreviewed;       300 AA.
AC   A9I9Y6;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Transcriptional regulator, LysR-family {ECO:0000313|EMBL:CAP44522.1};
GN   OrderedLocusNames=Bpet4174 {ECO:0000313|EMBL:CAP44522.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44522.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP44522.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000256|ARBA:ARBA00009437}.
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DR   EMBL; AM902716; CAP44522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I9Y6; -.
DR   STRING; 94624.Bpet4174; -.
DR   KEGG; bpt:Bpet4174; -.
DR   eggNOG; COG0583; Bacteria.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd08414; PBP2_LTTR_aromatics_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR30346:SF0; HCA OPERON TRANSCRIPTIONAL ACTIVATOR HCAR; 1.
DR   PANTHER; PTHR30346; TRANSCRIPTIONAL DUAL REGULATOR HCAR-RELATED; 1.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..58
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50931"
SQ   SEQUENCE   300 AA;  33215 MW;  6518039B86B0D9E7 CRC64;
     MELRHLRCFT ALAEELHFTR AAERLHIEQP PLSRAIKELE DELGVSLFDR DRRGTRLTPA
     GAAFLLDIRR LFTVLDQARE NVRAIAAGQK GSLRIAISDG AADQRLSAFL AHCREDEPEI
     EVRLSEVPLA DQLRGLRSGD FTIGFAHTAE VGDGICAEPI WQDPLVIAMP IRHELLAHKE
     IPLHKLGEHP LILCDPQVCE GYCRELTRLL RPLEREPNIV EHASSLDMML TLVGAGYGIG
     FTTAARMATS QRTDVVARPL ALDSAVINTY LLRPSNDALS PSLERFIARL RSQGGSAANQ
//
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