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Database: UniProt
Entry: B2FRU5_STRMK
LinkDB: B2FRU5_STRMK
Original site: B2FRU5_STRMK 
ID   B2FRU5_STRMK            Unreviewed;       299 AA.
AC   B2FRU5;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=LysR-family transcriptional regulator {ECO:0000313|EMBL:CAQ44650.1};
GN   OrderedLocusNames=Smlt1092 {ECO:0000313|EMBL:CAQ44650.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44650.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ44650.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ44650.1,
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; CAQ44650.1; -; Genomic_DNA.
DR   RefSeq; WP_005412489.1; NC_010943.1.
DR   AlphaFoldDB; B2FRU5; -.
DR   EnsemblBacteria; CAQ44650; CAQ44650; Smlt1092.
DR   KEGG; sml:Smlt1092; -.
DR   PATRIC; fig|522373.3.peg.1055; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_16_1_6; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd08474; PBP2_CrgA_like_5; 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; HTH-TYPE TRANSCRIPTIONAL REGULATOR; 1.
DR   PANTHER; PTHR30537:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATOR PGRR; 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          4..61
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50931"
SQ   SEQUENCE   299 AA;  32959 MW;  687155BD534B3DF3 CRC64;
     MPRENLNDLQ AFVHVAREGS FTKAAAQLGV SQSALSHAMR GLEQRLGVRL LTRTTRSVST
     TEAGARLLDT LGPRLAEIED GLAALAEYRE RPAGTIRINA TGHAAEYIAW PRLAPLLQQY
     PDLKVELAAD YGLADIVAER YDIGIRLGER LARDMVAVPI SPPLRMRVVG APGYFRQHVV
     PRHPDELADH NCVTLRLPTH GGLMPWDFGQ DGNELSVRVS GQWTFNTMGM TRAAALAGSG
     LAWLPEDQVQ PMLDDGRLQS VLDDWCPHFD GYYAYYPSRR HVTVAMRTVL DALRGPMAG
//
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