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P0A7C2

- LEXA_ECOLI

UniProt

P0A7C2 - LEXA_ECOLI

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Protein
LexA repressor
Gene
lexA, exrA, spr, tsl, umuA, b4043, JW4003
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publications

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 activity By similarity
Active sitei156 – 1561For autocatalytic cleavage activity By similarity

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

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 repressor (EC:3.4.21.88)
Gene namesi
Name:lexA
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 repressorUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP0A7C2.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.

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...

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 88 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

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