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Database: UniProt
Entry: B2FPD6_STRMK
LinkDB: B2FPD6_STRMK
Original site: B2FPD6_STRMK 
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
//
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