LRP_ECOLI
ID LRP_ECOLI Reviewed; 164 AA.
AC P0ACJ0; P19494;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Leucine-responsive regulatory protein;
GN Name=lrp; Synonyms=alsB, ihb, livR, oppI; OrderedLocusNames=b0889, JW0872;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2040596; DOI=10.1016/s0021-9258(18)99084-8;
RA Willins D.A., Ryan C., Platko J.V., Calvo J.M.;
RT "Characterization of Lrp, and Escherichia coli regulatory protein that
RT mediates a global response to leucine.";
RL J. Biol. Chem. 266:10768-10774(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ito K., Kawakami K., Nakamura Y.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=2115869; DOI=10.1128/jb.172.8.4563-4570.1990;
RA Platko J.V., Willins D.A., Calvo J.M.;
RT "The ilvIH operon of Escherichia coli is positively regulated.";
RL J. Bacteriol. 172:4563-4570(1990).
RN [7]
RP CHARACTERIZATION.
RX PubMed=1729203; DOI=10.1128/jb.174.1.108-115.1992;
RA Haney S.A., Platko J.V., Oxender D.L., Calvo J.M.;
RT "Lrp, a leucine-responsive protein, regulates branched-chain amino acid
RT transport genes in Escherichia coli.";
RL J. Bacteriol. 174:108-115(1992).
RN [8]
RP REVIEW.
RX PubMed=8212136; DOI=10.1016/0968-0004(93)90177-o;
RA D'Ari R., Lin R.T., Newman E.B.;
RT "The leucine-responsive regulatory protein: more than a regulator?";
RL Trends Biochem. Sci. 18:260-263(1993).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0ACJ0; P0ACJ0: lrp; NbExp=2; IntAct=EBI-1113316, EBI-1113316;
CC P0ACJ0; P0AFW4: rnk; NbExp=4; IntAct=EBI-1113316, EBI-553769;
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DR EMBL; M35869; AAA24089.1; -; Genomic_DNA.
DR EMBL; D11105; BAA01880.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73975.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35614.1; -; Genomic_DNA.
DR PIR; JH0412; RGECLR.
DR RefSeq; NP_415409.1; NC_000913.3.
DR RefSeq; WP_000228473.1; NZ_STEB01000006.1.
DR PDB; 2GQQ; X-ray; 3.20 A; A/B/C/D=2-164.
DR PDB; 2L4A; NMR; -; A=1-66.
DR PDBsum; 2GQQ; -.
DR PDBsum; 2L4A; -.
DR AlphaFoldDB; P0ACJ0; -.
DR BMRB; P0ACJ0; -.
DR SMR; P0ACJ0; -.
DR BioGRID; 4260697; 19.
DR BioGRID; 853295; 5.
DR DIP; DIP-35825N; -.
DR IntAct; P0ACJ0; 12.
DR STRING; 511145.b0889; -.
DR jPOST; P0ACJ0; -.
DR PaxDb; P0ACJ0; -.
DR PRIDE; P0ACJ0; -.
DR EnsemblBacteria; AAC73975; AAC73975; b0889.
DR EnsemblBacteria; BAA35614; BAA35614; BAA35614.
DR GeneID; 67414649; -.
DR GeneID; 949051; -.
DR KEGG; ecj:JW0872; -.
DR KEGG; eco:b0889; -.
DR PATRIC; fig|1411691.4.peg.1388; -.
DR EchoBASE; EB0542; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_091233_0_0_6; -.
DR InParanoid; P0ACJ0; -.
DR OMA; AGDENYI; -.
DR PhylomeDB; P0ACJ0; -.
DR BioCyc; EcoCyc:PD00353; -.
DR EvolutionaryTrace; P0ACJ0; -.
DR PRO; PR:P0ACJ0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000840; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoliWiki.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0006524; P:alanine catabolic process; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoliWiki.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0043201; P:response to leucine; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; DNA-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..164
FT /note="Leucine-responsive regulatory protein"
FT /id="PRO_0000111728"
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"
FT VARIANT 114
FT /note="D -> E (in lrp-1 mutant)"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2L4A"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2GQQ"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2GQQ"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2GQQ"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:2GQQ"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2GQQ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 103..120
FT /evidence="ECO:0007829|PDB:2GQQ"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2GQQ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2GQQ"
FT STRAND 142..155
FT /evidence="ECO:0007829|PDB:2GQQ"
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
