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P03023

- LACI_ECOLI

UniProt

P03023 - LACI_ECOLI

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Protein

Lactose operon repressor

Gene

lacI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi6 – 2520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00763.
ECOL316407:JW0336-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactose operon repressor
Gene namesi
Name:lacI
Ordered Locus Names:b0345, JW0336
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10525. lacI.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171Y → H: Broadening of specificity.
Mutagenesisi22 – 221R → N: Recognizes an operator variant.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Lactose operon repressorPRO_0000107963Add
BLAST

Proteomic databases

PRIDEiP03023.

Expressioni

Gene expression databases

GenevestigatoriP03023.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi849401. 1 interaction.
DIPiDIP-10079N.
IntActiP03023. 6 interactions.
MINTiMINT-6478062.
STRINGi511145.b0345.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116
Turni12 – 143
Helixi17 – 248
Turni25 – 273
Beta strandi28 – 303
Helixi33 – 4513
Helixi51 – 566
Helixi58 – 614
Beta strandi63 – 697
Helixi74 – 8916
Beta strandi93 – 986
Beta strandi101 – 1033
Helixi104 – 11512
Turni116 – 1183
Beta strandi122 – 1265
Helixi130 – 13910
Turni140 – 1423
Beta strandi145 – 1506
Beta strandi154 – 1563
Beta strandi158 – 1614
Helixi163 – 17715
Beta strandi181 – 1866
Helixi192 – 20716
Beta strandi213 – 2175
Helixi222 – 23413
Beta strandi240 – 2467
Helixi247 – 25913
Turni265 – 2673
Beta strandi268 – 2714
Helixi277 – 2815
Beta strandi282 – 2843
Beta strandi287 – 2904
Helixi293 – 30816
Beta strandi314 – 3196
Beta strandi322 – 3243
Beta strandi333 – 3386
Helixi339 – 35416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00433.
ProteinModelPortaliP03023.
SMRiP03023. Positions 1-360.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03023.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858HTH lacI-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH lacI-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1609.
HOGENOMiHOG000220179.
InParanoidiP03023.
OMAiNISYNES.
OrthoDBiEOG6SJJMM.
PhylomeDBiP03023.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamiPF00356. LacI. 1 hit.
[Graphical view]
PRINTSiPR00036. HTHLACI.
SMARTiSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
PROSITEiPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03023-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN
60 70 80 90 100
RVAQQLAGKQ SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE
110 120 130 140 150
RSGVEACKAA VHNLLAQRVS GLIINYPLDD QDAIAVEAAC TNVPALFLDV
160 170 180 190 200
SDQTPINSII FSHEDGTRLG VEHLVALGHQ QIALLAGPLS SVSARLRLAG
210 220 230 240 250
WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT AMLVANDQMA
260 270 280 290 300
LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS
310 320 330 340 350
VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA
360
RQVSRLESGQ
Length:360
Mass (Da):38,590
Last modified:July 19, 2003 - v3
Checksum:i347A8DEE92D736CB
GO

Sequence cautioni

The sequence AAB18069.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAB47270.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 2861L → S(PubMed:355891)Curated
Sequence conflicti286 – 2861L → S1 PublicationCurated
Sequence conflicti286 – 2861L → S(PubMed:1107032)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821Y → D in T41 mutant.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA93198. RPECL.
RefSeqiNP_414879.3. NC_000913.3.
YP_488639.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73448; AAC73448; b0345.
BAE76127; BAE76127; BAE76127.
GeneIDi12931674.
945007.
KEGGiecj:Y75_p0334.
eco:b0345.
PATRICi32115823. VBIEscCol129921_0353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A93198. RPECL.
RefSeqi NP_414879.3. NC_000913.3.
YP_488639.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CJG NMR - A/B 1-62 [» ]
1EFA X-ray 2.60 A/B/C 1-333 [» ]
1JWL X-ray 4.00 A/B/C 1-333 [» ]
1JYE X-ray 1.70 A 1-349 [» ]
1JYF X-ray 3.00 A 1-349 [» ]
1L1M NMR - A/B 1-62 [» ]
1LBG X-ray 4.80 A/B/C/D 1-360 [» ]
1LBH X-ray 3.20 A/B/C/D 1-360 [» ]
1LBI X-ray 2.70 A/B/C/D 1-360 [» ]
1LCC NMR - A 1-51 [» ]
1LCD NMR - A 1-51 [» ]
1LQC NMR - A 1-56 [» ]
1LTP model - L 62-323 [» ]
1OSL NMR - A/B 1-62 [» ]
1TLF X-ray 2.60 A/B/C/D 60-360 [» ]
1Z04 model - A/B/C/D 1-357 [» ]
2BJC NMR - A/B 1-62 [» ]
2KEI NMR - A/B 1-62 [» ]
2KEJ NMR - A/B 1-62 [» ]
2KEK NMR - A/B 1-62 [» ]
2P9H X-ray 2.00 A/B 62-330 [» ]
2PAF X-ray 3.50 A/B 62-330 [» ]
2PE5 X-ray 3.50 A/B/C 2-331 [» ]
3EDC X-ray 2.10 A/B/C/D 1-360 [» ]
DisProti DP00433.
ProteinModelPortali P03023.
SMRi P03023. Positions 1-360.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849401. 1 interaction.
DIPi DIP-10079N.
IntActi P03023. 6 interactions.
MINTi MINT-6478062.
STRINGi 511145.b0345.

Proteomic databases

PRIDEi P03023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73448 ; AAC73448 ; b0345 .
BAE76127 ; BAE76127 ; BAE76127 .
GeneIDi 12931674.
945007.
KEGGi ecj:Y75_p0334.
eco:b0345.
PATRICi 32115823. VBIEscCol129921_0353.

Organism-specific databases

EchoBASEi EB0520.
EcoGenei EG10525. lacI.

Phylogenomic databases

eggNOGi COG1609.
HOGENOMi HOG000220179.
InParanoidi P03023.
OMAi NISYNES.
OrthoDBi EOG6SJJMM.
PhylomeDBi P03023.

Enzyme and pathway databases

BioCyci EcoCyc:PD00763.
ECOL316407:JW0336-MONOMER.

Miscellaneous databases

EvolutionaryTracei P03023.
PROi P03023.

Gene expression databases

Genevestigatori P03023.

Family and domain databases

Gene3Di 1.10.260.40. 1 hit.
InterProi IPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view ]
Pfami PF00356. LacI. 1 hit.
[Graphical view ]
PRINTSi PR00036. HTHLACI.
SMARTi SM00354. HTH_LACI. 1 hit.
[Graphical view ]
SUPFAMi SSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
PROSITEi PS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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).

Entry informationi

Entry nameiLACI_ECOLI
AccessioniPrimary (citable) accession number: P03023
Secondary accession number(s): O09196
, P71309, Q2MC79, Q47338
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: October 29, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3