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Protein

Energy-dependent translational throttle protein EttA

Gene

ettA

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

A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E site where it modulates the state of the translating ribosome during subunit translocation. Stimulates dipeptide bond synthesis in the presence of ATP (cell in high energy state), but inhibits dipeptide synthesis in the presence of ADP (cell in low energy state), and thus may control translation in response to changing ATP levels (including during stationary phase). Following ATP hydrolysis is probably released allowing the ribosome to enter the elongation phase. Its specificity for the IC may be conferred by its recognition of features unique to tRNA(fMet).2 Publications

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 bindingi39 – 46ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi356 – 363ATP 2PROSITE-ProRule annotation8

<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

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • ribosome binding Source: EcoCyc
  • rRNA binding Source: UniProtKB-KW
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

<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 functionRNA-binding, rRNA-binding, tRNA-binding
Biological processProtein biosynthesis, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:YJJK-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:
Energy-dependent translational throttle protein EttA
Alternative name(s):
Translational regulatory factor EttA
<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:ettA
Synonyms:yjjK
Ordered Locus Names:b4391, JW4354
<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
EG12343 ettA

<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

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

Not essential it can be disrupted, its absence impairs fitness in long-term (up to 6 days) growth in stationary phase.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi188E → Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity; when associated with Q-470. 2 Publications1
Mutagenesisi470E → Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity; when associated with Q-188. 2 Publications1

<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 methionineiRemoved1 Publication
<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_00000931912 – 555Energy-dependent translational throttle protein EttAAdd BLAST554

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A9W3

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9W3

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

More...
PaxDbi
P0A9W3

PRoteomics IDEntifications database

More...
PRIDEi
P0A9W3

<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

Constitutively expressed, increases in stationary phase (at protein level).1 Publication

<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

Monomer at concentrations found in vivo, exists in a slowly reversible monomer-homodimer equilibrium. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P site containing tRNA(fMet).2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260798, 21 interactors

Database of interacting proteins

More...
DIPi
DIP-48138N

Protein interaction database and analysis system

More...
IntActi
P0A9W3, 13 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_4549

<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

1555
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
3J5Selectron microscopy7.50D1-555[»]
4FINX-ray2.40A/B1-555[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A9W3

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

More...
SMRi
P0A9W3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini6 – 259ABC transporter 1PROSITE-ProRule annotationAdd BLAST254
Domaini324 – 550ABC transporter 2PROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni95 – 139ArmAdd BLAST45
Regioni242 – 322PtIMAdd BLAST81

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The arm domain (residues 95-139) is inserted in the first ABC transporter domain. Its deletion abrogates the growth arrest and translation inhibition effect of the double Q-188/Q-470 mutation. When deleted impairs fitness in long-term (up to 6 days) growth in stationary phase (PubMed:24389466). Probably contacts ribosomal protein L1 (PubMed:24389465).2 Publications
The P-site tRNA interaction motif (PtIM domain, residues 242-322) probably interacts with the P site tRNA(fMet) as well as the 23S rRNA.

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C5H Bacteria
COG0488 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000271639

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9W3

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9W3

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR032781 ABC_tran_Xtn
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR022374 EttA
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR43858 PTHR43858, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00005 ABC_tran, 2 hits
PF12848 ABC_tran_Xtn, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03719 ABC_ABC_ChvD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 2 hits

<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.

P0A9W3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQFVYTMHR VGKVVPPKRH ILKNISLSFF PGAKIGVLGL NGAGKSTLLR
60 70 80 90 100
IMAGIDKDIE GEARPQPDIK IGYLPQEPQL NPEHTVRESI EEAVSEVVNA
110 120 130 140 150
LKRLDEVYAL YADPDADFDK LAAEQGRLEE IIQAHDGHNL NVQLERAADA
160 170 180 190 200
LRLPDWDAKI ANLSGGERRR VALCRLLLEK PDMLLLDEPT NHLDAESVAW
210 220 230 240 250
LERFLHDFEG TVVAITHDRY FLDNVAGWIL ELDRGEGIPW EGNYSSWLEQ
260 270 280 290 300
KDQRLAQEAS QEAARRKSIE KELEWVRQGT KGRQSKGKAR LARFEELNST
310 320 330 340 350
EYQKRNETNE LFIPPGPRLG DKVLEVSNLR KSYGDRLLID DLSFSIPKGA
360 370 380 390 400
IVGIIGPNGA GKSTLFRMIS GQEQPDSGTI TLGETVKLAS VDQFRDSMDN
410 420 430 440 450
SKTVWEEVSG GLDIMKIGNT EMPSRAYVGR FNFKGVDQGK RVGELSGGER
460 470 480 490 500
GRLHLAKLLQ VGGNMLLLDE PTNDLDIETL RALENALLEF PGCAMVISHD
510 520 530 540 550
RWFLDRIATH ILDYQDEGKV EFFEGNFTEY EEYKKRTLGA DALEPKRIKY

KRIAK
Length:555
Mass (Da):62,443
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:i444C7A3E2492D978
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA97287 differs from that shown. Reason: Frameshift at position 541.Curated
The sequence M69185 differs from that shown. Reason: Frameshift at position 49.Curated

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
U14003 Genomic DNA Translation: AAA97287.1 Frameshift.
U00096 Genomic DNA Translation: AAC77344.1
AP009048 Genomic DNA Translation: BAE78380.1
M69185 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
F65254

NCBI Reference Sequences

More...
RefSeqi
NP_418808.1, NC_000913.3
WP_000046749.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77344; AAC77344; b4391
BAE78380; BAE78380; BAE78380

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948909

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4354
eco:b4391

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2293

<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
U14003 Genomic DNA Translation: AAA97287.1 Frameshift.
U00096 Genomic DNA Translation: AAC77344.1
AP009048 Genomic DNA Translation: BAE78380.1
M69185 Genomic DNA No translation available.
PIRiF65254
RefSeqiNP_418808.1, NC_000913.3
WP_000046749.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J5Selectron microscopy7.50D1-555[»]
4FINX-ray2.40A/B1-555[»]
ProteinModelPortaliP0A9W3
SMRiP0A9W3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260798, 21 interactors
DIPiDIP-48138N
IntActiP0A9W3, 13 interactors
STRINGi316385.ECDH10B_4549

Proteomic databases

EPDiP0A9W3
jPOSTiP0A9W3
PaxDbiP0A9W3
PRIDEiP0A9W3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77344; AAC77344; b4391
BAE78380; BAE78380; BAE78380
GeneIDi948909
KEGGiecj:JW4354
eco:b4391
PATRICifig|1411691.4.peg.2293

Organism-specific databases

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

More...
EchoBASEi
EB2247
EcoGeneiEG12343 ettA

Phylogenomic databases

eggNOGiENOG4105C5H Bacteria
COG0488 LUCA
HOGENOMiHOG000271639
InParanoidiP0A9W3
PhylomeDBiP0A9W3

Enzyme and pathway databases

BioCyciEcoCyc:YJJK-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9W3

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR032781 ABC_tran_Xtn
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR022374 EttA
IPR027417 P-loop_NTPase
PANTHERiPTHR43858 PTHR43858, 1 hit
PfamiView protein in Pfam
PF00005 ABC_tran, 2 hits
PF12848 ABC_tran_Xtn, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SUPFAMiSSF52540 SSF52540, 2 hits
TIGRFAMsiTIGR03719 ABC_ABC_ChvD, 1 hit
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 2 hits

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 nameiETTA_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: P0A9W3
Secondary accession number(s): P37797, Q2M5S6
<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 19, 2005
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 105 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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