ID B2FPD6_STRMK Unreviewed; 305 AA.
AC B2FPD6;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=LysR-family transcriptional regulator {ECO:0000313|EMBL:CAQ44365.1};
GN OrderedLocusNames=Smlt0789 {ECO:0000313|EMBL:CAQ44365.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44365.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ44365.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ44365.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000256|ARBA:ARBA00009437}.
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DR EMBL; AM743169; CAQ44365.1; -; Genomic_DNA.
DR RefSeq; WP_005408112.1; NC_010943.1.
DR AlphaFoldDB; B2FPD6; -.
DR EnsemblBacteria; CAQ44365; CAQ44365; Smlt0789.
DR GeneID; 61464703; -.
DR KEGG; sml:Smlt0789; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_039613_16_0_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd08475; PBP2_CrgA_like_6; 1.
DR Gene3D; 3.40.190.290; -; 1.
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; PTHR30537:SF5; HTH-TYPE TRANSCRIPTIONAL ACTIVATOR TTDR-RELATED; 1.
DR PANTHER; PTHR30537; HTH-TYPE TRANSCRIPTIONAL REGULATOR; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000008840}.
FT DOMAIN 5..62
FT /note="HTH lysR-type"
FT /evidence="ECO:0000259|PROSITE:PS50931"
SQ SEQUENCE 305 AA; 32757 MW; 78508B9EEACC8C37 CRC64;
MLPTERLRGI EAFVATADAG SFTAAAERLH LTSSAVGKTI ARLEARLGAR LFERSTRRLR
LTEAGEGFYR TCVRVLGELA DAESVLVSHA DAPVGRLRVD APATFGRLKV WPLLLQLAAE
FPQLHPQVTF SDRFSDLAED GVDLAVRIGG PEPLPATLGS RLLGYECLRF CASPAYLLRH
GQPRSAAELA GHDGVLFGRA DGSIGPWQVA DGRQRSTPLQ ARARLVVGSA EAQVAAVEAG
FGIAQLATWL VDDALARGSL VSILPSLDCR GLPLRLLWPQ GRQRLPRVDV ALDRLGAGLQ
IDPPR
//