Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A7C2

- LEXA_ECOLI

UniProt

P0A7C2 - LEXA_ECOLI

Protein

LexA repressor

Gene

lexA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.2 PublicationsUniRule annotation

    Catalytic activityi

    Hydrolysis of Ala-|-Gly bond in repressor LexA.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei84 – 852Cleavage; by autolysis
    Active sitei119 – 1191For autocatalytic cleavage activityUniRule annotation
    Active sitei156 – 1561For autocatalytic cleavage activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi28 – 4821H-T-H motifUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: EcoliWiki
    2. serine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. DNA repair Source: UniProtKB-HAMAP
    3. DNA replication Source: UniProtKB-HAMAP
    4. negative regulation of transcription, DNA-templated Source: EcoliWiki
    5. SOS response Source: EcoCyc
    6. transcription, DNA-templated Source: EcoCyc

    Keywords - Molecular functioni

    Hydrolase, Repressor

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PD00205.
    ECOL316407:JW4003-MONOMER.

    Protein family/group databases

    MEROPSiS24.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LexA repressorUniRule annotation (EC:3.4.21.88UniRule annotation)
    Gene namesi
    Name:lexAUniRule annotation
    Synonyms:exrA, spr, tsl, umuA
    Ordered Locus Names:b4043, JW4003
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10533. lexA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 202202LexA repressorPRO_0000170031Add
    BLAST

    Keywords - PTMi

    Autocatalytic cleavage

    Proteomic databases

    PaxDbiP0A7C2.
    PRIDEiP0A7C2.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7C2.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsEP0A7W11EBI-553416,EBI-543949

    Protein-protein interaction databases

    DIPiDIP-51082N.
    IntActiP0A7C2. 11 interactions.
    MINTiMINT-1314348.
    STRINGi511145.b4043.

    Structurei

    Secondary structure

    1
    202
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 2217
    Helixi28 – 347
    Helixi40 – 5213
    Beta strandi55 – 584
    Beta strandi60 – 645
    Beta strandi66 – 683
    Beta strandi74 – 796
    Helixi91 – 933
    Beta strandi94 – 985
    Helixi102 – 1043
    Beta strandi105 – 1073
    Beta strandi111 – 1144
    Helixi121 – 1233
    Beta strandi130 – 1356
    Beta strandi143 – 1497
    Beta strandi152 – 16110
    Beta strandi164 – 1685
    Beta strandi172 – 1743
    Beta strandi177 – 1804
    Turni181 – 1833
    Beta strandi186 – 19712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JHCX-ray2.00A68-202[»]
    1JHEX-ray2.50A/B68-202[»]
    1JHFX-ray1.80A/B1-202[»]
    1JHHX-ray2.10A/B1-202[»]
    1LEANMR-A1-84[»]
    1LEBNMR-A1-84[»]
    1MVDmodel-A/B1-202[»]
    1QAAmodel-A/B1-202[»]
    3JSOX-ray2.29A/B1-202[»]
    3JSPX-ray2.90A/B1-202[»]
    3K3RX-ray3.20E/F1-202[»]
    ProteinModelPortaliP0A7C2.
    SMRiP0A7C2. Positions 1-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7C2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S24 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1974.
    HOGENOMiHOG000232167.
    KOiK01356.
    OMAiMSMKNIG.
    OrthoDBiEOG6JHRHJ.
    PhylomeDBiP0A7C2.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.10.109.10. 1 hit.
    HAMAPiMF_00015. LexA.
    InterProiIPR006200. LexA.
    IPR006199. LexA_DNA-bd_dom.
    IPR028360. Peptidase_S24/S26_b-rbn.
    IPR006197. Peptidase_S24_LexA.
    IPR019759. Peptidase_S24_S26.
    IPR015927. Peptidase_S24_S26A/B/C.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01726. LexA_DNA_bind. 1 hit.
    PF00717. Peptidase_S24. 1 hit.
    [Graphical view]
    PRINTSiPR00726. LEXASERPTASE.
    SUPFAMiSSF51306. SSF51306. 1 hit.
    TIGRFAMsiTIGR00498. lexA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A7C2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL    50
    ARKGVIEIVS GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV 100
    DPSLFKPNAD FLLRVSGMSM KDIGIMDGDL LAVHKTQDVR NGQVVVARID 150
    DEVTVKRLKK QGNKVELLPE NSEFKPIVVD LRQQSFTIEG LAVGVIRNGD 200
    WL 202
    Length:202
    Mass (Da):22,358
    Last modified:July 21, 1986 - v1
    Checksum:i7E8816A32C19EE71
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851G → D in lexA3, resistant to cleavage.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01643 Genomic DNA. Translation: AAA24067.1.
    U00006 Genomic DNA. Translation: AAC43137.1.
    U00096 Genomic DNA. Translation: AAC77013.1.
    AP009048 Genomic DNA. Translation: BAE78045.1.
    L02362 Genomic DNA. Translation: AAA24068.1.
    PIRiA90808. ILEC.
    RefSeqiNP_418467.1. NC_000913.3.
    YP_492186.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77013; AAC77013; b4043.
    BAE78045; BAE78045; BAE78045.
    GeneIDi12932724.
    948544.
    KEGGiecj:Y75_p3930.
    eco:b4043.
    PATRICi32123623. VBIEscCol129921_4160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01643 Genomic DNA. Translation: AAA24067.1 .
    U00006 Genomic DNA. Translation: AAC43137.1 .
    U00096 Genomic DNA. Translation: AAC77013.1 .
    AP009048 Genomic DNA. Translation: BAE78045.1 .
    L02362 Genomic DNA. Translation: AAA24068.1 .
    PIRi A90808. ILEC.
    RefSeqi NP_418467.1. NC_000913.3.
    YP_492186.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JHC X-ray 2.00 A 68-202 [» ]
    1JHE X-ray 2.50 A/B 68-202 [» ]
    1JHF X-ray 1.80 A/B 1-202 [» ]
    1JHH X-ray 2.10 A/B 1-202 [» ]
    1LEA NMR - A 1-84 [» ]
    1LEB NMR - A 1-84 [» ]
    1MVD model - A/B 1-202 [» ]
    1QAA model - A/B 1-202 [» ]
    3JSO X-ray 2.29 A/B 1-202 [» ]
    3JSP X-ray 2.90 A/B 1-202 [» ]
    3K3R X-ray 3.20 E/F 1-202 [» ]
    ProteinModelPortali P0A7C2.
    SMRi P0A7C2. Positions 1-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-51082N.
    IntActi P0A7C2. 11 interactions.
    MINTi MINT-1314348.
    STRINGi 511145.b4043.

    Protein family/group databases

    MEROPSi S24.001.

    Proteomic databases

    PaxDbi P0A7C2.
    PRIDEi P0A7C2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77013 ; AAC77013 ; b4043 .
    BAE78045 ; BAE78045 ; BAE78045 .
    GeneIDi 12932724.
    948544.
    KEGGi ecj:Y75_p3930.
    eco:b4043.
    PATRICi 32123623. VBIEscCol129921_4160.

    Organism-specific databases

    EchoBASEi EB0528.
    EcoGenei EG10533. lexA.

    Phylogenomic databases

    eggNOGi COG1974.
    HOGENOMi HOG000232167.
    KOi K01356.
    OMAi MSMKNIG.
    OrthoDBi EOG6JHRHJ.
    PhylomeDBi P0A7C2.

    Enzyme and pathway databases

    BioCyci EcoCyc:PD00205.
    ECOL316407:JW4003-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7C2.
    PROi P0A7C2.

    Gene expression databases

    Genevestigatori P0A7C2.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.10.109.10. 1 hit.
    HAMAPi MF_00015. LexA.
    InterProi IPR006200. LexA.
    IPR006199. LexA_DNA-bd_dom.
    IPR028360. Peptidase_S24/S26_b-rbn.
    IPR006197. Peptidase_S24_LexA.
    IPR019759. Peptidase_S24_S26.
    IPR015927. Peptidase_S24_S26A/B/C.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01726. LexA_DNA_bind. 1 hit.
    PF00717. Peptidase_S24. 1 hit.
    [Graphical view ]
    PRINTSi PR00726. LEXASERPTASE.
    SUPFAMi SSF51306. SSF51306. 1 hit.
    TIGRFAMsi TIGR00498. lexA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the lexA gene of E. coli."
      Horii T., Ogawa T., Ogawa H.
      Cell 23:689-697(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the lexA gene of Escherichia coli K-12."
      Markham B.E., Little J.W., Mount D.W.
      Nucleic Acids Res. 9:4149-4161(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT LEXA3.
      Strain: K12.
    3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Genetic analysis of the LexA repressor: isolation and characterization of LexA(Def) mutant proteins."
      Oertel-Buchheit P., Lamerichs R.M., Schnarr M., Granger-Schnarr M.
      Mol. Gen. Genet. 223:40-48(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
    7. "Organization of the lexA gene of Escherichia coli and nucleotide sequence of the regulatory region."
      Miki T., Ebina Y., Kishi F., Nakazawa A.
      Nucleic Acids Res. 9:529-543(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    8. Lilley P.E., Dixon N.E.
      Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-202.
      Strain: K12.
    9. "Purified lexA protein is a repressor of the recA and lexA genes."
      Little J.W., Mount D.W., Yanisch-Perron C.R.
      Proc. Natl. Acad. Sci. U.S.A. 78:4199-4203(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: FUNCTION.
    11. "The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study."
      Lamerichs R.M.J.N., Padilla A., Boelens R., Kaptein R., Ottleben G., Rueterjans H., Granger-Schnarr M., Oertel P., Schnarr M.
      Proc. Natl. Acad. Sci. U.S.A. 86:6863-6867(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    12. "Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy."
      Fogh R.H., Ottleben G., Rueterjans H., Schnarr M., Boelens R., Kaptein R.
      EMBO J. 13:3936-3944(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    13. Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiLEXA_ECOLI
    AccessioniPrimary (citable) accession number: P0A7C2
    Secondary accession number(s): P03033, Q2M6R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3