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
//