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UniProtKB - P0A7C2 (LEXA_ECOLI)

Entry version 125 (08 May 2019)
Sequence version 1 (21 Jul 1986)
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Protein

LexA repressor

Gene

lexA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847).The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in response to DNA damaging agents that is mediated by RecA and LexA (PubMed:22412352).UniRule annotation4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei119For autocatalytic cleavage activityUniRule annotation1
Active sitei156For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi28 – 48H-T-H motifUniRule annotationAdd BLAST21

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Hydrolase, Repressor
Biological processDNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PD00205
ECOL316407:JW4003-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.88 2026

Protein family/group databases

MEROPS protease database

More...MEROPSi		S24.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
LexA repressorUniRule annotation (EC:3.4.21.88UniRule annotation)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:lexAUniRule annotation
Synonyms:exrA, spr, tsl, umuA
Ordered Locus Names:b4043, JW4003
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10533 lexA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001700311 – 202LexA repressorAdd BLAST202

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei84 – 85Cleavage; by autolysis2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A7C2

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7C2

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0A7C2

PRoteomics IDEntifications database

More...PRIDEi		P0A7C2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...CollecTFi		EXPREG_000007a0

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4261718, 11 interactors

Database of interacting proteins

More...DIPi		DIP-51082N

Protein interaction database and analysis system

More...IntActi		P0A7C2, 11 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4043

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0A7C2

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A7C2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105DS7 Bacteria
COG1974 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000232167

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7C2

KEGG Orthology (KO)

More...KOi		K01356

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7C2

Family and domain databases

Conserved Domains Database

More...CDDi		cd06529 S24_LexA-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00015 LexA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006200 LexA
IPR039418 LexA-like
IPR036286 LexA/Signal_pep-like_sf
IPR006199 LexA_DNA-bd_dom
IPR006197 Peptidase_S24_LexA
IPR015927 Peptidase_S24_S26A/B/C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01726 LexA_DNA_bind, 1 hit
PF00717 Peptidase_S24, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00726 LEXASERPTASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46785 SSF46785, 1 hit
SSF51306 SSF51306, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00498 lexA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A7C2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL 
        60         70         80         90        100
ARKGVIEIVS GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV 
       110        120        130        140        150
DPSLFKPNAD FLLRVSGMSM KDIGIMDGDL LAVHKTQDVR NGQVVVARID 
       160        170        180        190        200
DEVTVKRLKK QGNKVELLPE NSEFKPIVVD LRQQSFTIEG LAVGVIRNGD 

WL
Length:202
Mass (Da):22,358
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7E8816A32C19EE71
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti85G → D in lexA3, resistant to cleavage. Increased sensitivity to hydroxyurea. 2 Publications1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

Protein sequence database of the Protein Information Resource

More...PIRi		A90808 ILEC

NCBI Reference Sequences

More...RefSeqi		NP_418467.1, NC_000913.3
WP_000646078.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77013; AAC77013; b4043
BAE78045; BAE78045; BAE78045

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948544

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW4003
eco:b4043

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.4160

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000646078.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
SMRiP0A7C2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261718, 11 interactors
DIPiDIP-51082N
IntActiP0A7C2, 11 interactors
STRINGi511145.b4043

Protein family/group databases

MEROPSiS24.001

Proteomic databases

EPDiP0A7C2
jPOSTiP0A7C2
PaxDbiP0A7C2
PRIDEiP0A7C2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77013; AAC77013; b4043
BAE78045; BAE78045; BAE78045
GeneIDi948544
KEGGiecj:JW4003
eco:b4043
PATRICifig|511145.12.peg.4160

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0528
EcoGeneiEG10533 lexA

Phylogenomic databases

eggNOGiENOG4105DS7 Bacteria
COG1974 LUCA
HOGENOMiHOG000232167
InParanoidiP0A7C2
KOiK01356
PhylomeDBiP0A7C2

Enzyme and pathway databases

BioCyciEcoCyc:PD00205
ECOL316407:JW4003-MONOMER
BRENDAi3.4.21.88 2026

Miscellaneous databases

EvolutionaryTraceiP0A7C2

Protein Ontology

More...PROi		PR:P0A7C2

Gene expression databases

CollecTFiEXPREG_000007a0

Family and domain databases

CDDicd06529 S24_LexA-like, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_00015 LexA, 1 hit
InterProiView protein in InterPro
IPR006200 LexA
IPR039418 LexA-like
IPR036286 LexA/Signal_pep-like_sf
IPR006199 LexA_DNA-bd_dom
IPR006197 Peptidase_S24_LexA
IPR015927 Peptidase_S24_S26A/B/C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF01726 LexA_DNA_bind, 1 hit
PF00717 Peptidase_S24, 1 hit
PRINTSiPR00726 LEXASERPTASE
SUPFAMiSSF46785 SSF46785, 1 hit
SSF51306 SSF51306, 1 hit
TIGRFAMsiTIGR00498 lexA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLEXA_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A7C2
Secondary accession number(s): P03033, Q2M6R1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 8, 2019
This is version 125 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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