LRP_SHIFL
ID LRP_SHIFL Reviewed; 164 AA.
AC P0ACJ3; P19494;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Leucine-responsive regulatory protein;
GN Name=lrp; OrderedLocusNames=SF0848, S0889;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Mediates a global response to leucine. Exogenous leucine
CC affects the expression of a number of different operons; lrp mediates
CC this effect for at least some of these operons. For example it is
CC regulator of the branched-chain amino acid transport genes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE005674; AAN42481.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16353.1; -; Genomic_DNA.
DR RefSeq; NP_706774.2; NC_004337.2.
DR RefSeq; WP_000228473.1; NZ_WPGW01000037.1.
DR AlphaFoldDB; P0ACJ3; -.
DR BMRB; P0ACJ3; -.
DR SMR; P0ACJ3; -.
DR STRING; 198214.SF0848; -.
DR EnsemblBacteria; AAN42481; AAN42481; SF0848.
DR EnsemblBacteria; AAP16353; AAP16353; S0889.
DR GeneID; 1023815; -.
DR GeneID; 67414649; -.
DR KEGG; sfl:SF0848; -.
DR KEGG; sfx:S0889; -.
DR PATRIC; fig|198214.7.peg.978; -.
DR HOGENOM; CLU_091233_0_0_6; -.
DR OMA; AGDENYI; -.
DR OrthoDB; 1844486at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProt.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR PRINTS; PR00033; HTHASNC.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS00519; HTH_ASNC_1; 1.
DR PROSITE; PS50956; HTH_ASNC_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..164
FT /note="Leucine-responsive regulatory protein"
FT /id="PRO_0000111737"
FT DOMAIN 12..73
FT /note="HTH asnC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT DNA_BIND 31..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ SEQUENCE 164 AA; 18887 MW; 2952FB9347A2725C CRC64;
MVDSKKRPGK DLDRIDRNIL NELQKDGRIS NVELSKRVGL SPTPCLERVR RLERQGFIQG
YTALLNPHYL DASLLVFVEI TLNRGAPDVF EQFNTAVQKL EEIQECHLVS GDFDYLLKTR
VPDMSAYRKL LGETLLRLPG VNDTRTYVVM EEVKQSNRLV IKTR