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Protein

Protein RecA

Gene

recA

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

Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. 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).4 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The rate of DNA-strand exchange is stimulated by RadA.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi67 – 74ATPUniRule annotation1 Publication8

<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

  • ATP binding Source: UniProtKB-UniRule
  • damaged DNA binding Source: UniProtKB-UniRule
  • DNA-dependent ATPase activity Source: UniProtKB-UniRule
  • single-stranded DNA binding Source: EcoliWiki

GO - Biological processi

  • cell motility Source: EcoliWiki
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA recombination Source: CACAO
  • DNA repair Source: UniProtKB-UniRule
  • response to ionizing radiation Source: EcoCyc
  • response to radiation Source: EcoCyc
  • SOS response Source: CACAO

<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
Biological processDNA damage, DNA recombination, DNA repair, SOS response, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10823-MONOMER
MetaCyc:EG10823-MONOMER

<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:
Protein RecAUniRule annotation
Alternative name(s):
Recombinase AUniRule 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:recAUniRule annotation
Synonyms:lexB, recH, rnmB, tif, umuB, zab
Ordered Locus Names:b2699, JW2669
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
EG10823 recA

<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

  • cytosol Source: GO_Central

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Triple mazE-mazF-recA mutant cells no longer undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization.1 Publication

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3434

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00001227032 – 353Protein RecAAdd BLAST352

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A7G6

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

More...
PaxDbi
P0A7G6

PRoteomics IDEntifications database

More...
PRIDEi
P0A7G6

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A7G6

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by DNA damage, repressed by LexA (PubMed:10760155). Induced in response to low temperature (PubMed:8898389). Sensitive to temperature through changes in the linking number of the DNA. Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389). 5.1-fold induced by hydroxyurea treatment (at protein level) (PubMed:20005847). mRNA levels are repressed in a mazE-mazF-mediated manner (PubMed:22412352).4 Publications

<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

Polymerizes non-specifically on ssDNA to form filaments; filament formation requires ATP or ATP-gamma-S. Interacts with and activates LexA leading to autocatalytic cleavage of LexA, which derepresses the SOS regulon and activates DNA repair. Interacts with the C-terminus of RecB, facilitating loading of RecA onto ssDNA at chi sites. Interaction is decreased by ATP.3 Publications

<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

WithEntry#Exp.IntActNotes
mutLP233673EBI-370331,EBI-554913

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259218, 460 interactors

Database of interacting proteins

More...
DIPi
DIP-31832N

Protein interaction database and analysis system

More...
IntActi
P0A7G6, 33 interactors

STRING: functional protein association networks

More...
STRINGi
316407.85675524

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A7G6

<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

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0A7G6

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

More...
SMRi
P0A7G6

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
P0A7G6

<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 RecA family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C68 Bacteria
COG0468 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000264120

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A7G6

KEGG Orthology (KO)

More...
KOi
K03553

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A7G6

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00983 recA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.250.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00268 RecA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR013765 DNA_recomb/repair_RecA
IPR020584 DNA_recomb/repair_RecA_CS
IPR027417 P-loop_NTPase
IPR020588 RecA_ATP-bd
IPR023400 RecA_C
IPR020587 RecA_monomer-monomer_interface

The PANTHER Classification System

More...
PANTHERi
PTHR22942:SF1 PTHR22942:SF1, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00154 RecA, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00142 RECA

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF54752 SSF54752, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02012 tigrfam_recA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00321 RECA_1, 1 hit
PS50162 RECA_2, 1 hit
PS50163 RECA_3, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7G6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI
60 70 80 90 100
ALGAGGLPMG RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL
110 120 130 140 150
DPIYARKLGV DIDNLLCSQP DTGEQALEIC DALARSGAVD VIVVDSVAAL
160 170 180 190 200
TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA GNLKQSNTLL IFINQIRMKI
210 220 230 240 250
GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG SETRVKVVKN
260 270 280 290 300
KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG
310 320 330 340 350
QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN

EDF
Length:353
Mass (Da):37,973
Last modified:January 23, 2007 - v2
<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:i866EF8F83BE32A36
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti191Missing AA sequence (PubMed:7588783).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V00328 Genomic DNA Translation: CAA23618.1
U00096 Genomic DNA Translation: AAC75741.1
AP009048 Genomic DNA Translation: BAA16561.2

Protein sequence database of the Protein Information Resource

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PIRi
G65049 RQECA

NCBI Reference Sequences

More...
RefSeqi
NP_417179.1, NC_000913.3
WP_000963143.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75741; AAC75741; b2699
BAA16561; BAA16561; BAA16561

Database of genes from NCBI RefSeq genomes

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GeneIDi
947170

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2669
eco:b2699

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4043

<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
V00328 Genomic DNA Translation: CAA23618.1
U00096 Genomic DNA Translation: AAC75741.1
AP009048 Genomic DNA Translation: BAA16561.2
PIRiG65049 RQECA
RefSeqiNP_417179.1, NC_000913.3
WP_000963143.1, NZ_LN832404.1

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
1AA3NMR-A269-331[»]
1N03electron microscopy20.00A/B/C/D/E/F/G2-353[»]
1REAX-ray2.70A2-353[»]
1U94X-ray1.90A2-353[»]
1U98X-ray2.00A2-353[»]
1U99X-ray2.60A2-353[»]
1XMSX-ray2.10A2-353[»]
1XMVX-ray1.90A2-353[»]
2REBX-ray2.30A2-353[»]
2RECelectron microscopy-A/B/C/D/E/F1-353[»]
3CMTX-ray3.15A/D2-335[»]
3CMUX-ray4.20A2-335[»]
3CMVX-ray4.30A/B/C/D/E/F/G/H2-335[»]
3CMWX-ray2.80A/C2-335[»]
3CMXX-ray3.40A/D2-335[»]
4TWZX-ray2.80A2-353[»]
ProteinModelPortaliP0A7G6
SMRiP0A7G6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259218, 460 interactors
DIPiDIP-31832N
IntActiP0A7G6, 33 interactors
STRINGi316407.85675524

Chemistry databases

BindingDBiP0A7G6
ChEMBLiCHEMBL3434

2D gel databases

SWISS-2DPAGEiP0A7G6

Proteomic databases

EPDiP0A7G6
PaxDbiP0A7G6
PRIDEiP0A7G6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75741; AAC75741; b2699
BAA16561; BAA16561; BAA16561
GeneIDi947170
KEGGiecj:JW2669
eco:b2699
PATRICifig|1411691.4.peg.4043

Organism-specific databases

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

More...
EchoBASEi
EB0816
EcoGeneiEG10823 recA

Phylogenomic databases

eggNOGiENOG4105C68 Bacteria
COG0468 LUCA
HOGENOMiHOG000264120
InParanoidiP0A7G6
KOiK03553
PhylomeDBiP0A7G6

Enzyme and pathway databases

BioCyciEcoCyc:EG10823-MONOMER
MetaCyc:EG10823-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7G6

Protein Ontology

More...
PROi
PR:P0A7G6

Family and domain databases

CDDicd00983 recA, 1 hit
Gene3Di3.30.250.10, 1 hit
HAMAPiMF_00268 RecA, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR013765 DNA_recomb/repair_RecA
IPR020584 DNA_recomb/repair_RecA_CS
IPR027417 P-loop_NTPase
IPR020588 RecA_ATP-bd
IPR023400 RecA_C
IPR020587 RecA_monomer-monomer_interface
PANTHERiPTHR22942:SF1 PTHR22942:SF1, 1 hit
PfamiView protein in Pfam
PF00154 RecA, 1 hit
PRINTSiPR00142 RECA
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF54752 SSF54752, 1 hit
TIGRFAMsiTIGR02012 tigrfam_recA, 1 hit
PROSITEiView protein in PROSITE
PS00321 RECA_1, 1 hit
PS50162 RECA_2, 1 hit
PS50163 RECA_3, 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 nameiRECA_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: P0A7G6
Secondary accession number(s): P03017, P26347, P78213
<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: January 23, 2007
Last modified: November 7, 2018
This is version 126 of the entry and version 2 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, Direct protein sequencing, 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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