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UniProtKB - P30870 (GLNE_ECOLI)

Entry version 138 (08 May 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme

Gene

glnE

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

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia (PubMed:8412694). When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity (PubMed:4920894, PubMed:9312015). Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity (PubMed:4893578, PubMed:4920873, PubMed:4934180, PubMed:9312015, PubMed:14766310). The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell (PubMed:8412694).8 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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+4 PublicationsNote: Can also use Mn2+.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 adenylation activity is stimulated by glutamine and PII (GlnB), and inhibited by 2-oxoglutarate (PubMed:4867671, PubMed:4920894, PubMed:33597, PubMed:9312015). Deadenylation activity is stimulated by PII-UMP (GlnB-UMP) and 2-oxoglutarate, and inhibited by glutamine (PubMed:4893578, PubMed:4934180, PubMed:33597, PubMed:9312015, PubMed:14766310).7 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=4 µM for adenylyl1 Publication
  2. KM=5 µM for [L-glutamate:ammonia ligase (ADP-forming)]1 Publication
  3. KM=150 µM for ATP1 Publication

    pH dependencei

    Optimum pH is between 7.3 and 7.6 (PubMed:4893578, PubMed:4920894). The enzyme is stable between pH 4 and 9 (PubMed:4920894).2 Publications

    <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 functionMultifunctional enzyme, Nucleotidyltransferase, Transferase
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:GLNE-MONOMER
    ECOL316407:JW3025-MONOMER
    MetaCyc:GLNE-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.7.42 2026

    <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:
    Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeCurated
    Alternative name(s):
    ATP:glutamine synthetase adenylyltransferase1 Publication
    ATase1 Publication
    Including the following 2 domains:
    Glutamine synthetase adenylyl-L-tyrosine phosphorylase1 Publication (EC:2.7.7.894 Publications1 Publication)
    Alternative name(s):
    Adenylyl removase1 Publication
    Short name:
    AR1 Publication
    Short name:
    AT-N1 Publication
    Short name:
    AT-N4401 Publication
    Short name:
    P-I1 Publication
    Glutamine synthetase adenylyl transferase1 Publication (EC:2.7.7.421 Publication1 Publication)
    Alternative name(s):
    Adenylyl transferase1 Publication
    Short name:
    AT1 Publication
    Short name:
    AT-C1 Publication
    <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:glnE1 Publication
    Ordered Locus Names:b3053, JW3025
    <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    		EG11602 glnE

    <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_00002092441 – 946Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzymeAdd BLAST946

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P30870

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

    More...    PaxDbi    		P30870

    PRoteomics IDEntifications database

    More...    PRIDEi    		P30870

    <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.1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261515, 4 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-9780N

    Protein interaction database and analysis system

    More...    IntActi    		P30870, 2 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3053

    <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

    1946
    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
    1V4AX-ray2.00A1-440[»]
    3K7DX-ray2.40A/B449-946[»]

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

    More...    SMRi    		P30870

    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    		P30870

    <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

    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>Regioni1 – 440Adenylyl removase1 PublicationAdd BLAST440
    Regioni441 – 448Linker1 Publication8
    Regioni449 – 946Adenylyl transferase1 PublicationAdd BLAST498

    <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 GlnE family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105CE6 Bacteria
    COG1391 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000256491

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P30870

    KEGG Orthology (KO)

    More...    KOi    		K00982

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P30870

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_00802 GlnE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR023057 GlnE
    IPR005190 GlnE_rpt_dom
    IPR013546 PII_UdlTrfase/GS_AdlTrfase

    The PANTHER Classification System

    More...    PANTHERi    		PTHR30621 PTHR30621, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF08335 GlnD_UR_UTase, 2 hits
    PF03710 GlnE, 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.

    P30870-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP 
            60         70         80         90        100
    EWLTELESQP PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR 
           110        120        130        140        150
    IAWAQTLALV TEESILQQLS YLAETLIVAA RDWLYDACCR EWGTPCNAQG 
           160        170        180        190        200
    EAQPLLILGM GKLGGGELNF SSDIDLIFAW PEHGCTQGGR RELDNAQFFT 
           210        220        230        240        250
    RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA ALEDYYQEQG 
           260        270        280        290        300
    RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK 
           310        320        330        340        350
    GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL 
           360        370        380        390        400
    PTLSAIAELH LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL 
           410        420        430        440        450
    NRARLAWAMD FADWPQLTGA LTAHMTNVRR VFNELIGDDE SETQEESLSE 
           460        470        480        490        500
    QWRELWQDAL QEDDTTPVLA HLSEDDRKQV LTLIADFRKE LDKRTIGPRG 
           510        520        530        540        550
    RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT YLELLSEFPA 
           560        570        580        590        600
    ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ 
           610        620        630        640        650
    YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA 
           660        670        680        690        700
    EAMIDAVVQQ AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS 
           710        720        730        740        750
    DLDLIFLHDC PMDAMTDGER EIDGRQFYLR LAQRIMHLFS TRTSSGILYE 
           760        770        780        790        800
    VDARLRPSGA AGMLVTSAEA FADYQKNEAW TWEHQALVRA RVVYGDPQLT 
           810        820        830        840        850
    AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR DRFDIKADEG 
           860        870        880        890        900
    GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL 
           910        920        930        940 
    TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE
    Length:946
    Mass (Da):108,418
    Last modified:November 1, 1997 - 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:i6FD2D7BDC619DB83
    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 conflicti524Missing in CAA79892 (PubMed:8412694).Curated1
    Sequence conflicti624 – 625QL → PV in CAA79892 (PubMed:8412694).Curated2

    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
    		Z21844 Genomic DNA Translation: CAA79892.1
    U00096 Genomic DNA Translation: AAC76089.1
    AP009048 Genomic DNA Translation: BAE77104.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		C65093

    NCBI Reference Sequences

    More...    RefSeqi    		NP_417525.1, NC_000913.3
    WP_001301081.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76089; AAC76089; b3053
    BAE77104; BAE77104; BAE77104

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947552

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW3025
    eco:b3053

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.3678

    <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
    		Z21844 Genomic DNA Translation: CAA79892.1
    U00096 Genomic DNA Translation: AAC76089.1
    AP009048 Genomic DNA Translation: BAE77104.1
    PIRiC65093
    RefSeqiNP_417525.1, NC_000913.3
    WP_001301081.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1V4AX-ray2.00A1-440[»]
    3K7DX-ray2.40A/B449-946[»]
    SMRiP30870
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261515, 4 interactors
    DIPiDIP-9780N
    IntActiP30870, 2 interactors
    STRINGi511145.b3053

    Proteomic databases

    jPOSTiP30870
    PaxDbiP30870
    PRIDEiP30870

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76089; AAC76089; b3053
    BAE77104; BAE77104; BAE77104
    GeneIDi947552
    KEGGiecj:JW3025
    eco:b3053
    PATRICifig|1411691.4.peg.3678

    Organism-specific databases

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

    More...    EchoBASEi    		EB1559
    EcoGeneiEG11602 glnE

    Phylogenomic databases

    eggNOGiENOG4105CE6 Bacteria
    COG1391 LUCA
    HOGENOMiHOG000256491
    InParanoidiP30870
    KOiK00982
    PhylomeDBiP30870

    Enzyme and pathway databases

    BioCyciEcoCyc:GLNE-MONOMER
    ECOL316407:JW3025-MONOMER
    MetaCyc:GLNE-MONOMER
    BRENDAi2.7.7.42 2026

    Miscellaneous databases

    EvolutionaryTraceiP30870

    Protein Ontology

    More...    PROi    		PR:P30870

    Family and domain databases

    HAMAPiMF_00802 GlnE, 1 hit
    InterProiView protein in InterPro
    IPR023057 GlnE
    IPR005190 GlnE_rpt_dom
    IPR013546 PII_UdlTrfase/GS_AdlTrfase
    PANTHERiPTHR30621 PTHR30621, 1 hit
    PfamiView protein in Pfam
    PF08335 GlnD_UR_UTase, 2 hits
    PF03710 GlnE, 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 nameiGLNE_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: P30870
    Secondary accession number(s): P78107, Q2M9F2
    <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 1, 1993
    Last sequence update: November 1, 1997
    Last modified: May 8, 2019
    This is version 138 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, 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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