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P03023 (LACI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactose operon repressor
Gene names
Name:lacI
Ordered Locus Names:b0345, JW0336
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Repressor of the lactose operon. Binds allolactose as an inducer.

Subunit structure

Homotetramer.

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 similarities

Contains 1 HTH lacI-type DNA-binding domain.

Sequence caution

The sequence AAB18069.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAB47270.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Lactose operon repressor
PRO_0000107963

Regions

Domain1 – 5858HTH lacI-type
DNA binding6 – 2520H-T-H motif

Natural variations

Natural variant2821Y → D in T41 mutant.

Experimental info

Mutagenesis171Y → H: Broadening of specificity.
Mutagenesis221R → N: Recognizes an operator variant.
Sequence conflict2861L → S Ref.1
Sequence conflict2861L → S Ref.4
Sequence conflict2861L → S Ref.7

Secondary structure

................................................................. 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03023 [UniParc].

Last modified July 19, 2003. Version 3.
Checksum: 347A8DEE92D736CB

FASTA36038,590
        10         20         30         40         50         60 
MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ 

        70         80         90        100        110        120 
SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS 

       130        140        150        160        170        180 
GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ 

       190        200        210        220        230        240 
QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT 

       250        260        270        280        290        300 
AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS 

       310        320        330        340        350        360 
VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the lacI gene."
Farabaugh P.J.
Nature 274:765-769(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Chen J., Matthews K.K.S.M.
Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Marsh S.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequence of minutes 4-25 of Escherichia coli."
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.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Amino-acid sequence of lac repressor from Escherichia coli. Isolation, sequence analysis and sequence assembly of tryptic peptides and cyanogen-bromide fragments."
Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.
Eur. J. Biochem. 59:491-509(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360.
[8]"Lac repressor. Specific proteolytic destruction of the NH 2 -terminal region and loss of the deoxyribonucleic acid-binding activity."
Platt T., Files J.G., Weber K.
J. Biol. Chem. 248:110-121(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
[9]"Reinitiation of a lac repressor fragment at a condon other than AUG."
Ganem D., Miller J.H., Files J.G., Platt T., Weber K.
Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86.
[10]"Missense mutation in the lacI gene of Escherichia coli. Inferences on the structure of the repressor protein."
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.
J. Mol. Biol. 200:239-251(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
[11]"Mechanism of Lac repressor switch-off: orientation of the Lac repressor DNA-binding domain is reversed upon inducer binding."
Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.
FEBS Lett. 375:27-30(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-35.
[12]"Mutant lac repressors with new specificities hint at rules for protein-DNA recognition."
Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B., Mueller-Hill B.
EMBO J. 9:615-621(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"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."
Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.
J. Mol. Biol. 240:421-433(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[14]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[15]"A model of the lac repressor-operator complex based on physical and genetic data."
Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B., Mueller-Hill B.
Eur. J. Biochem. 198:411-419(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[16]"Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving."
Shin J.A., Ebright R.H., Dervan P.B.
Nucleic Acids Res. 19:5233-5236(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 1-56.
[17]"The interaction of lac repressor headpiece with its operator: an NMR view."
Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H., Kaptein R.
Protein Seq. Data Anal. 1:487-498(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[18]"H NMR study of a complex between the lac repressor headpiece and a 22 base pair symmetric lac operator."
Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H., Kaptein R., Buck F., Fera B., Rueterjans H.
Biochemistry 28:2985-2991(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]"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."
Slijper M., Bonvin A.M., Boelens R., Kaptein R.
J. Mol. Biol. 259:761-773(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-56.
[20]"The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator."
Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R., Kaptein R.
Structure 7:1483-1492(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-62.
[21]"Crystal structure of the lactose operon repressor and its complexes with DNA and inducer."
Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C., Schumacher M.A., Brennan R.G., Lu P.
Science 271:1247-1254(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00294 Genomic DNA. Translation: CAA23569.1.
X58469 Genomic DNA. Translation: CAA41383.1.
U86347 Genomic DNA. Translation: AAB47270.1. Different initiation.
J01636 Genomic DNA. Translation: AAA24052.1.
U72488 Genomic DNA. Translation: AAB36549.1.
U78872 Genomic DNA. Translation: AAB37348.1.
U78873 Genomic DNA. Translation: AAB37351.1.
U78874 Genomic DNA. Translation: AAB37354.1.
U73857 Genomic DNA. Translation: AAB18069.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73448.1.
AP009048 Genomic DNA. Translation: BAE76127.1.
PIRRPECL. A93198.
RefSeqNP_414879.3. NC_000913.3.
YP_488639.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJGNMR-A/B1-62[»]
1EFAX-ray2.60A/B/C1-333[»]
1JWLX-ray4.00A/B/C1-333[»]
1JYEX-ray1.70A1-349[»]
1JYFX-ray3.00A1-349[»]
1L1MNMR-A/B1-62[»]
1LBGX-ray4.80A/B/C/D1-360[»]
1LBHX-ray3.20A/B/C/D1-360[»]
1LBIX-ray2.70A/B/C/D1-360[»]
1LCCNMR-A1-51[»]
1LCDNMR-A1-51[»]
1LQCNMR-A1-56[»]
1LTPmodel-L62-323[»]
1OSLNMR-A/B1-62[»]
1TLFX-ray2.60A/B/C/D60-360[»]
1Z04model-A/B/C/D1-357[»]
2BJCNMR-A/B1-62[»]
2KEINMR-A/B1-62[»]
2KEJNMR-A/B1-62[»]
2KEKNMR-A/B1-62[»]
2P9HX-ray2.00A/B62-330[»]
2PAFX-ray3.50A/B62-330[»]
2PE5X-ray3.50A/B/C2-331[»]
3EDCX-ray2.10A/B/C/D1-360[»]
DisProtDP00433.
ProteinModelPortalP03023.
SMRP03023. Positions 1-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid849401. 1 interaction.
DIPDIP-10079N.
IntActP03023. 6 interactions.
MINTMINT-6478062.
STRING511145.b0345.

Proteomic databases

PRIDEP03023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73448; AAC73448; b0345.
BAE76127; BAE76127; BAE76127.
GeneID12931674.
945007.
KEGGecj:Y75_p0334.
eco:b0345.
PATRIC32115823. VBIEscCol129921_0353.

Organism-specific databases

EchoBASEEB0520.
EcoGeneEG10525. lacI.

Phylogenomic databases

eggNOGCOG1609.
HOGENOMHOG000220179.
OMAMTSISAR.
OrthoDBEOG6SJJMM.
ProtClustDBPRK09526.

Enzyme and pathway databases

BioCycEcoCyc:PD00763.
ECOL316407:JW0336-MONOMER.

Gene expression databases

GenevestigatorP03023.

Family and domain databases

Gene3D1.10.260.40. 1 hit.
InterProIPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamPF00356. LacI. 1 hit.
[Graphical view]
PRINTSPR00036. HTHLACI.
SMARTSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
PROSITEPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03023.
PROP03023.

Entry information

Entry nameLACI_ECOLI
AccessionPrimary (citable) accession number: P03023
Secondary accession number(s): O09196 expand/collapse secondary AC list , P71309, Q2MC79, Q47338
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: March 19, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene