LEUO_ECOLI
ID LEUO_ECOLI Reviewed; 314 AA.
AC P10151; P75640;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=HTH-type transcriptional regulator LeuO;
GN Name=leuO; OrderedLocusNames=b0076, JW0075;
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=3413113; DOI=10.1073/pnas.85.18.6602;
RA Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C.;
RT "A large family of bacterial activator proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6602-6606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 291-314.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC STRAIN=K12;
RX PubMed=3519576; DOI=10.1128/jb.166.3.1113-1117.1986;
RA Haughn G.W., Wessler S.R., Gemmill R.M., Calvo J.M.;
RT "High A + T content conserved in DNA sequences upstream of leuABCD in
RT Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 166:1113-1117(1986).
RN [6]
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).
RN [7]
RP ROLE AS A TRANSCRIPTIONAL REGULATOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / CSH26;
RX PubMed=9422614; DOI=10.1128/jb.180.1.190-193.1998;
RA Ueguchi C., Ohta T., Seto C., Suzuki T., Mizuno T.;
RT "The leuO gene product has a latent ability to relieve bgl silencing in
RT Escherichia coli.";
RL J. Bacteriol. 180:190-193(1998).
RN [8]
RP DNA-BINDING.
RC STRAIN=CSH50;
RX PubMed=18055596; DOI=10.1128/jb.01447-07;
RA Stratmann T., Madhusudan S., Schnetz K.;
RT "Regulation of the yjjQ-bglJ operon, encoding LuxR-type transcription
RT factors, and the divergent yjjP gene by H-NS and LeuO.";
RL J. Bacteriol. 190:926-935(2008).
RN [9]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, FUNCTION AS A TRANSCRIPTIONAL
RP REPRESSOR, DNA-BINDING, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
RN [10]
RP ROLE AS A TRANSCRIPTIONAL REGULATOR, DNA-BINDING, AND INDEPENDENCE OF
RP BGLJ-RCSB.
RX PubMed=20952573; DOI=10.1128/jb.00807-10;
RA Venkatesh G.R., Kembou Koungni F.C., Paukner A., Stratmann T.,
RA Blissenbach B., Schnetz K.;
RT "BglJ-RcsB heterodimers relieve repression of the Escherichia coli bgl
RT operon by H-NS.";
RL J. Bacteriol. 192:6456-6464(2010).
RN [11]
RP ANTAGONIZES H-NS, AND ROLE IN CRISPR EXPRESSION.
RC STRAIN=K12;
RX PubMed=20659289; DOI=10.1111/j.1365-2958.2010.07315.x;
RA Westra E.R., Pul U., Heidrich N., Jore M.M., Lundgren M., Stratmann T.,
RA Wurm R., Raine A., Mescher M., Van Heereveld L., Mastop M., Wagner E.G.,
RA Schnetz K., Van Der Oost J., Wagner R., Brouns S.J.;
RT "H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12
RT can be relieved by the transcription activator LeuO.";
RL Mol. Microbiol. 77:1380-1393(2010).
CC -!- FUNCTION: A global transcription factor. Activates transcription of the
CC 9 following operons; yjjQ-bglJ, yjjP, acrEF, ybdO, yjcRQP, casABCDE12,
CC rhsD-ybbC, fepE and gltF, in most cases it probably interferes with
CC silencing by H-NS and activates transcription. Represses transcription
CC of the 3 following operons; uxaCA, sdaCB and btsT. H-NS repression of
CC the bgl operon, leading to the ability to metabolize some beta-
CC glucosides. It also directly activates the bgl operon. Activation is H-
CC NS and BglJ-RcsB independent. {ECO:0000269|PubMed:19429622,
CC ECO:0000269|PubMed:20659289, ECO:0000269|PubMed:20952573,
CC ECO:0000269|PubMed:9422614}.
CC -!- INDUCTION: Gene expression is repressed by H-NS, activated by itself.
CC More highly expressed in minimal than rich medium, poorly expressed in
CC exoponential growth, levels increase in stationary phase (at protein
CC level). {ECO:0000269|PubMed:19429622}.
CC -!- DISRUPTION PHENOTYPE: Has no effect on leucine biosynthesis nor on bgl
CC operon silencing. {ECO:0000269|PubMed:9422614}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA38853.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M21150; AAA85299.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38853.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73187.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96645.2; -; Genomic_DNA.
DR EMBL; M12891; AAA83880.1; ALT_INIT; Genomic_DNA.
DR PIR; D64729; D64729.
DR RefSeq; NP_414618.4; NC_000913.3.
DR RefSeq; WP_001115472.1; NZ_STEB01000010.1.
DR PDB; 6GZ0; X-ray; 1.52 A; A=109-314.
DR PDB; 6GZ1; X-ray; 1.74 A; A=109-314.
DR PDB; 6GZ2; X-ray; 1.94 A; A=109-314.
DR PDBsum; 6GZ0; -.
DR PDBsum; 6GZ1; -.
DR PDBsum; 6GZ2; -.
DR AlphaFoldDB; P10151; -.
DR SMR; P10151; -.
DR BioGRID; 4259484; 4.
DR BioGRID; 853278; 3.
DR IntAct; P10151; 5.
DR STRING; 511145.b0076; -.
DR PaxDb; P10151; -.
DR PRIDE; P10151; -.
DR EnsemblBacteria; AAC73187; AAC73187; b0076.
DR EnsemblBacteria; BAB96645; BAB96645; BAB96645.
DR GeneID; 949034; -.
DR KEGG; ecj:JW0075; -.
DR KEGG; eco:b0076; -.
DR PATRIC; fig|1411691.4.peg.2205; -.
DR EchoBASE; EB0526; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_039613_39_0_6; -.
DR InParanoid; P10151; -.
DR OMA; ICSPLDI; -.
DR PhylomeDB; P10151; -.
DR BioCyc; EcoCyc:PD00519; -.
DR PRO; PR:P10151; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..314
FT /note="HTH-type transcriptional regulator LeuO"
FT /id="PRO_0000105660"
FT DOMAIN 22..79
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 39..58
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT CONFLICT 291..314
FT /note="Missing (in Ref. 1; AAA85299 and 2; CAA38853)"
FT /evidence="ECO:0000305"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:6GZ2"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6GZ1"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6GZ0"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6GZ0"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6GZ1"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:6GZ0"
SQ SEQUENCE 314 AA; 35695 MW; 25605FA08C1073E3 CRC64;
MPEVQTDHPE TAELSKPQLR MVDLNLLTVF DAVMQEQNIT RAAHVLGMSQ PAVSNAVARL
KVMFNDELFV RYGRGIQPTA RAFQLFGSVR QALQLVQNEL PGSGFEPASS ERVFHLCVCS
PLDSILTSQI YNHIEQIAPN IHVMFKSSLN QNTEHQLRYQ ETEFVISYED FHRPEFTSVP
LFKDEMVLVA SKNHPTIKGP LLKHDVYNEQ HAAVSLDRFA SFSQPWYDTV DKQASIAYQG
MAMMSVLSVV SQTHLVAIAP RWLAEEFAES LELQVLPLPL KQNSRTCYLS WHEAAGRDKG
HQWMEEQLVS ICKR
