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Lactose operon repressor

 LACI_ECOLI              Reviewed;         360 AA.
P03023; O09196; P71309; Q2MC79; Q47338;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
19-JUL-2003, sequence version 3.
28-MAR-2018, entry version 179.
RecName: Full=Lactose operon repressor;
Name=lacI; OrderedLocusNames=b0345, JW0336;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=355891; DOI=10.1038/274765a0;
Farabaugh P.J.;
"Sequence of the lacI gene.";
Nature 274:765-769(1978).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chen J., Matthews K.K.S.M.;
Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Marsh S.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360.
PubMed=1107032; DOI=10.1111/j.1432-1033.1975.tb02477.x;
Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.;
"Amino-acid sequence of lac repressor from Escherichia coli.
Isolation, sequence analysis and sequence assembly of tryptic peptides
and cyanogen-bromide fragments.";
Eur. J. Biochem. 59:491-509(1975).
[8]
PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
PubMed=4571224;
Platt T., Files J.G., Weber K.;
"Lac repressor. Specific proteolytic destruction of the NH 2 -terminal
region and loss of the deoxyribonucleic acid-binding activity.";
J. Biol. Chem. 248:110-121(1973).
[9]
PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86.
PubMed=4594037; DOI=10.1073/pnas.70.11.3165;
Ganem D., Miller J.H., Files J.G., Platt T., Weber K.;
"Reinitiation of a lac repressor fragment at a condon other than
AUG.";
Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
PubMed=3286877; DOI=10.1016/0022-2836(88)90237-9;
Gordon A.J.E., Burns P.A., Fix D.F., Yatagai F., Allen F.L.,
Horsfall M.J., Halliday J.A., Gray J., Bernelot-Moens C.,
Glickman B.W.;
"Missense mutation in the lacI gene of Escherichia coli. Inferences on
the structure of the repressor protein.";
J. Mol. Biol. 200:239-251(1988).
[11]
PROTEIN SEQUENCE OF 1-35.
PubMed=7498473; DOI=10.1016/0014-5793(95)01153-6;
Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.;
"Mechanism of Lac repressor switch-off: orientation of the Lac
repressor DNA-binding domain is reversed upon inducer binding.";
FEBS Lett. 375:27-30(1995).
[12]
MUTAGENESIS.
PubMed=2178920;
Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B.,
Mueller-Hill B.;
"Mutant lac repressors with new specificities hint at rules for
protein-DNA recognition.";
EMBO J. 9:615-621(1990).
[13]
MUTAGENESIS.
PubMed=8046748; DOI=10.1006/jmbi.1994.1458;
Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.;
"Genetic studies of the lac repressor. XIV. Analysis of 4000 altered
Escherichia coli lac repressors reveals essential and non-essential
residues, as well as 'spacers' which do not require a specific
sequence.";
J. Mol. Biol. 240:421-433(1994).
[14]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[15]
3D-STRUCTURE MODELING.
PubMed=2040302; DOI=10.1111/j.1432-1033.1991.tb16030.x;
Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B.,
Mueller-Hill B.;
"A model of the lac repressor-operator complex based on physical and
genetic data.";
Eur. J. Biochem. 198:411-419(1991).
[16]
3D-STRUCTURE MODELING OF 1-56.
PubMed=1923807; DOI=10.1093/nar/19.19.5233;
Shin J.A., Ebright R.H., Dervan P.B.;
"Orientation of the Lac repressor DNA binding domain in complex with
the left lac operator half site characterized by affinity cleaving.";
Nucleic Acids Res. 19:5233-5236(1991).
[17]
STRUCTURE BY NMR.
PubMed=3064080;
Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H.,
Kaptein R.;
"The interaction of lac repressor headpiece with its operator: an NMR
view.";
Protein Seq. Data Anal. 1:487-498(1988).
[18]
STRUCTURE BY NMR.
PubMed=2742823; DOI=10.1021/bi00433a037;
Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H.,
Kaptein R., Buck F., Fera B., Rueterjans H.;
"H NMR study of a complex between the lac repressor headpiece and a 22
base pair symmetric lac operator.";
Biochemistry 28:2985-2991(1989).
[19]
STRUCTURE BY NMR OF 1-56.
PubMed=8683581; DOI=10.1006/jmbi.1996.0356;
Slijper M., Bonvin A.M., Boelens R., Kaptein R.;
"Refined structure of lac repressor headpiece (1-56) determined by
relaxation matrix calculations from 2D and 3D NOE data: change of
tertiary structure upon binding to the lac operator.";
J. Mol. Biol. 259:761-773(1996).
[20]
STRUCTURE BY NMR OF 1-62.
PubMed=10647179; DOI=10.1016/S0969-2126(00)88339-2;
Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R.,
Kaptein R.;
"The solution structure of Lac repressor headpiece 62 complexed to a
symmetrical lac operator.";
Structure 7:1483-1492(1999).
[21]
X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
PubMed=8638105; DOI=10.1126/science.271.5253.1247;
Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C.,
Schumacher M.A., Brennan R.G., Lu P.;
"Crystal structure of the lactose operon repressor and its complexes
with DNA and inducer.";
Science 271:1247-1254(1996).
-!- FUNCTION: Repressor of the lactose operon. Binds allolactose as an
inducer.
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-909231, EBI-909231;
-!- MISCELLANEOUS: Removing residues 1-59 results in loss of DNA-
binding activity but retains tetrameric structure and inducer-
binding activity. Deleting residues 340-360 results in loss of
tetramer formation, but retains dimer formation, inducer-binding
activity, and DNA-binding activity (if residues 1-59 are present).
-!- SEQUENCE CAUTION:
Sequence=AAB18069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAB47270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; V00294; CAA23569.1; -; Genomic_DNA.
EMBL; X58469; CAA41383.1; -; Genomic_DNA.
EMBL; U86347; AAB47270.1; ALT_INIT; Genomic_DNA.
EMBL; J01636; AAA24052.1; -; Genomic_DNA.
EMBL; U72488; AAB36549.1; -; Genomic_DNA.
EMBL; U78872; AAB37348.1; -; Genomic_DNA.
EMBL; U78873; AAB37351.1; -; Genomic_DNA.
EMBL; U78874; AAB37354.1; -; Genomic_DNA.
EMBL; U73857; AAB18069.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73448.1; -; Genomic_DNA.
EMBL; AP009048; BAE76127.1; -; Genomic_DNA.
PIR; A93198; RPECL.
RefSeq; NP_414879.3; NC_000913.3.
RefSeq; WP_000805902.1; NZ_LN832404.1.
PDB; 1CJG; NMR; -; A/B=1-62.
PDB; 1EFA; X-ray; 2.60 A; A/B/C=1-333.
PDB; 1JWL; X-ray; 4.00 A; A/B/C=1-333.
PDB; 1JYE; X-ray; 1.70 A; A=1-349.
PDB; 1JYF; X-ray; 3.00 A; A=1-349.
PDB; 1L1M; NMR; -; A/B=1-62.
PDB; 1LBG; X-ray; 4.80 A; A/B/C/D=1-360.
PDB; 1LBH; X-ray; 3.20 A; A/B/C/D=1-360.
PDB; 1LBI; X-ray; 2.70 A; A/B/C/D=1-360.
PDB; 1LCC; NMR; -; A=1-51.
PDB; 1LCD; NMR; -; A=1-51.
PDB; 1LQC; NMR; -; A=1-56.
PDB; 1LTP; Model; -; L=62-323.
PDB; 1OSL; NMR; -; A/B=1-62.
PDB; 1TLF; X-ray; 2.60 A; A/B/C/D=60-360.
PDB; 1Z04; Model; -; A/B/C/D=1-357.
PDB; 2BJC; NMR; -; A/B=1-62.
PDB; 2KEI; NMR; -; A/B=1-62.
PDB; 2KEJ; NMR; -; A/B=1-62.
PDB; 2KEK; NMR; -; A/B=1-62.
PDB; 2P9H; X-ray; 2.00 A; A/B=62-330.
PDB; 2PAF; X-ray; 3.50 A; A/B=62-330.
PDB; 2PE5; X-ray; 3.50 A; A/B/C=2-331.
PDB; 3EDC; X-ray; 2.10 A; A/B/C/D=1-360.
PDB; 4RZS; X-ray; 2.71 A; A/B/C/D=2-360.
PDB; 4RZT; X-ray; 3.10 A; A/B/C/D=2-360.
PDBsum; 1CJG; -.
PDBsum; 1EFA; -.
PDBsum; 1JWL; -.
PDBsum; 1JYE; -.
PDBsum; 1JYF; -.
PDBsum; 1L1M; -.
PDBsum; 1LBG; -.
PDBsum; 1LBH; -.
PDBsum; 1LBI; -.
PDBsum; 1LCC; -.
PDBsum; 1LCD; -.
PDBsum; 1LQC; -.
PDBsum; 1LTP; -.
PDBsum; 1OSL; -.
PDBsum; 1TLF; -.
PDBsum; 1Z04; -.
PDBsum; 2BJC; -.
PDBsum; 2KEI; -.
PDBsum; 2KEJ; -.
PDBsum; 2KEK; -.
PDBsum; 2P9H; -.
PDBsum; 2PAF; -.
PDBsum; 2PE5; -.
PDBsum; 3EDC; -.
PDBsum; 4RZS; -.
PDBsum; 4RZT; -.
ProteinModelPortal; P03023; -.
SMR; P03023; -.
BioGrid; 4260668; 11.
BioGrid; 849401; 1.
DIP; DIP-10079N; -.
IntAct; P03023; 6.
MINT; P03023; -.
STRING; 316385.ECDH10B_1357; -.
DrugBank; DB01862; Isopropyl beta-D-thiogalactopyranoside.
DrugBank; DB08297; ORTHONITROPHENYL-BETA-D-FUCOPYRANOSIDE.
PaxDb; P03023; -.
PRIDE; P03023; -.
EnsemblBacteria; AAC73448; AAC73448; b0345.
EnsemblBacteria; BAE76127; BAE76127; BAE76127.
GeneID; 945007; -.
KEGG; ecj:JW0336; -.
KEGG; eco:b0345; -.
PATRIC; fig|511145.12.peg.353; -.
EchoBASE; EB0520; -.
EcoGene; EG10525; lacI.
eggNOG; ENOG4105ETE; Bacteria.
eggNOG; COG1609; LUCA.
HOGENOM; HOG000220179; -.
InParanoid; P03023; -.
OMA; RLRYEGW; -.
PhylomeDB; P03023; -.
BioCyc; EcoCyc:PD00763; -.
EvolutionaryTrace; P03023; -.
PRO; PR:P03023; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0000986; F:bacterial-type proximal promoter sequence-specific DNA binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001141; F:transcriptional repressor activity, bacterial-type RNA polymerase proximal promoter sequence-specific DNA binding; IDA:EcoCyc.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd01392; HTH_LacI; 1.
InterPro; IPR000843; HTH_LacI.
InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00356; LacI; 1.
PRINTS; PR00036; HTHLACI.
SMART; SM00354; HTH_LACI; 1.
SUPFAM; SSF47413; SSF47413; 1.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00356; HTH_LACI_1; 1.
PROSITE; PS50932; HTH_LACI_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA-binding; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 360 Lactose operon repressor.
/FTId=PRO_0000107963.
DOMAIN 1 58 HTH lacI-type. {ECO:0000255|PROSITE-
ProRule:PRU00111}.
DNA_BIND 6 25 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00111}.
VARIANT 282 282 Y -> D (in T41 mutant).
MUTAGEN 17 17 Y->H: Broadening of specificity.
MUTAGEN 22 22 R->N: Recognizes an operator variant.
CONFLICT 286 286 L -> S (in Ref. 1, 4 and 7).
{ECO:0000305}.
HELIX 6 11 {ECO:0000244|PDB:1EFA}.
TURN 12 14 {ECO:0000244|PDB:1EFA}.
HELIX 17 24 {ECO:0000244|PDB:1EFA}.
TURN 25 27 {ECO:0000244|PDB:1LQC}.
STRAND 28 30 {ECO:0000244|PDB:1CJG}.
HELIX 33 45 {ECO:0000244|PDB:1EFA}.
HELIX 51 56 {ECO:0000244|PDB:1EFA}.
HELIX 58 61 {ECO:0000244|PDB:2BJC}.
STRAND 63 69 {ECO:0000244|PDB:1JYE}.
HELIX 74 89 {ECO:0000244|PDB:1JYE}.
STRAND 93 98 {ECO:0000244|PDB:1JYE}.
STRAND 101 103 {ECO:0000244|PDB:1JYE}.
HELIX 104 115 {ECO:0000244|PDB:1JYE}.
TURN 116 118 {ECO:0000244|PDB:1JYE}.
STRAND 122 126 {ECO:0000244|PDB:1JYE}.
HELIX 130 139 {ECO:0000244|PDB:1JYE}.
TURN 140 142 {ECO:0000244|PDB:1JYE}.
STRAND 145 150 {ECO:0000244|PDB:1JYE}.
STRAND 154 156 {ECO:0000244|PDB:1JYE}.
STRAND 158 161 {ECO:0000244|PDB:1JYE}.
HELIX 163 177 {ECO:0000244|PDB:1JYE}.
STRAND 181 186 {ECO:0000244|PDB:1JYE}.
HELIX 192 207 {ECO:0000244|PDB:1JYE}.
STRAND 213 217 {ECO:0000244|PDB:1JYE}.
HELIX 222 234 {ECO:0000244|PDB:1JYE}.
STRAND 240 246 {ECO:0000244|PDB:1JYE}.
HELIX 247 259 {ECO:0000244|PDB:1JYE}.
TURN 265 267 {ECO:0000244|PDB:1JYE}.
STRAND 268 271 {ECO:0000244|PDB:1JYE}.
HELIX 277 281 {ECO:0000244|PDB:1JYE}.
STRAND 282 284 {ECO:0000244|PDB:1JYE}.
STRAND 287 290 {ECO:0000244|PDB:1JYE}.
HELIX 293 308 {ECO:0000244|PDB:1JYE}.
STRAND 314 319 {ECO:0000244|PDB:1JYE}.
STRAND 322 324 {ECO:0000244|PDB:1JYE}.
STRAND 333 338 {ECO:0000244|PDB:1LBH}.
HELIX 339 354 {ECO:0000244|PDB:3EDC}.
SEQUENCE 360 AA; 38590 MW; 347A8DEE92D736CB CRC64;
MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ
SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS
GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ
QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT
AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS
VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ


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