ID Q2KX56_BORA1 Unreviewed; 476 AA.
AC Q2KX56;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=GntR-family transcriptional regulator {ECO:0000313|EMBL:CAJ50157.1};
GN OrderedLocusNames=BAV2547 {ECO:0000313|EMBL:CAJ50157.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50157.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ50157.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ50157.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
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DR EMBL; AM167904; CAJ50157.1; -; Genomic_DNA.
DR RefSeq; WP_012418200.1; NC_010645.1.
DR AlphaFoldDB; Q2KX56; -.
DR GeneID; 41394386; -.
DR KEGG; bav:BAV2547; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_1_4; -.
DR OrthoDB; 9804020at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR PANTHER; PTHR46577:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..67
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 476 AA; 52655 MW; 701D41F2FAC38945 CRC64;
MNQRLYRAIR EAILDGTLPG DTRLPASRDL AAELSVARNT VVHVYAQLQA EGYTRSRQGN
GTFVTASVPD AYLATGRSRR HQAHAPAGPV LSERGARIVD RASASPYQWG AFMPGVPDVT
EFPHRKFGRI FSALWRKPPP ELLTYAYGGG LPALREALAE HLALTRSVDC DAEQIIITEG
SHQAIDLATR MLGSAGDVAW IENPGYWGAR TVLSANGVRI APQPVDEEGM LLPATAEIDE
PPRFIFVTPS HQYPLGTVMS LARRRQLLAL ARRWGSWIIE DDYDSEFRFS GRPISSLQGL
EPDAPVIYLG TFSKTLYPGL RVGYLVLPKN LAAAFQAGHA ELYREGHLMT HAALATFIAE
GHYAAHIRRM RMLYARRRAI LVNLIERRLG AQWLLRDSSE AGLHLILNLP QDLDDNAVVD
VARARGVLTR PLSRYYAGSE PARRGLLLGY ACVPESQIAR KFEILLDSLT EVARRA
//
