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P03023

- LACI_ECOLI

UniProt

P03023 - LACI_ECOLI

Protein

Lactose operon repressor

Gene

lacI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (19 Jul 2003)
      Previous versions | rss
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    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

    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

    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.
    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

    MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN    50
    RVAQQLAGKQ SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE 100
    RSGVEACKAA VHNLLAQRVS GLIINYPLDD QDAIAVEAAC TNVPALFLDV 150
    SDQTPINSII FSHEDGTRLG VEHLVALGHQ QIALLAGPLS SVSARLRLAG 200
    WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT AMLVANDQMA 250
    LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS 300
    VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA 350
    RQVSRLESGQ 360
    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.
    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

    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 1, 2014
    This is version 153 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