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UniProtKB - P08839 (PT1_ECOLI)

Entry version 203 (07 Apr 2021)
Sequence version 1 (01 Nov 1988)
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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

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

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (PubMed:7876255, PubMed:12705838, PubMed:17053069). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors (PubMed:12705838).3 Publications

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.1 Publication
Enzyme I of the sugar PTS has been shown to phosphorylate NPr of the nitrogen-metabolic PTS, though much less efficiently than it does HPr. This process may link carbon and nitrogen assimilation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by oxalate.1 Publication

<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

Kcat is 3830 min(-1) with PEP as substrate. Kcat is 370 min(-1) with ZFPEP as substrate. Kcat is 285 min(-1) with ZMePEP as substrate. Kcat is 15.8 min(-1) with ZClPEP as substrate. Kcat is 2.8 min(-1) with EClPEP as substrate.1 Publication
  1. KM=0.11 mM for ZFPEP1 Publication
  2. KM=0.12 mM for EClPEP1 Publication
  3. KM=0.14 mM for PEP1 Publication
  4. KM=0.25 mM for ZClPEP1 Publication
  5. KM=0.43 mM for ZMePEP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei189Tele-phosphohistidine intermediate2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei296PEPBy similarity1
    Binding sitei332PEP1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi431Magnesium1 Publication1
    Metal bindingi455Magnesium1 Publication1
    Binding sitei465PEPBy similarity1
    Active sitei502Proton donor1 Publication1 Publication1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionKinase, Transferase
    Biological processPhosphotransferase system, Sugar transport, Transport
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.3.9, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P08839

    Protein family/group databases

    Transport Classification Database

    More...    TCDBi    		8.A.7.1.1, the phosphotransferase system enzyme i (ei) family

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Phosphoenolpyruvate-protein phosphotransferase1 Publication (EC:2.7.3.91 Publication)
    Alternative name(s):
    Phosphotransferase system, enzyme I1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ptsI1 Publication
    Ordered Locus Names:b2416, JW2409
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    <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

    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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi189H → A: Very strong decrease of the affinity and catalytic efficiency for PEP. Inactive; when associated with A-502. 1 Publication1
    Mutagenesisi502C → A: Inactive; when associated with A-189. 1 Publication1

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001470671 – 575Phosphoenolpyruvate-protein phosphotransferaseAdd BLAST575

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P08839

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

    More...    PaxDbi    		P08839

    PRoteomics IDEntifications database

    More...    PRIDEi    		P08839

    2D gel databases

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

    More...    SWISS-2DPAGEi    		P08839

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260570, 520 interactors
    851219, 3 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10603N

    Protein interaction database and analysis system

    More...    IntActi    		P08839, 14 interactors

    Molecular INTeraction database

    More...    MINTi    		P08839

    STRING: functional protein association networks

    More...    STRINGi    		511145.b2416

    <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

    1575
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...    BMRBi    		P08839

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

    More...    SMRi    		P08839

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P08839

    <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>Regioni454 – 455PEP binding1 Publication2

    <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 N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.1 Publication

    <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 PEP-utilizing enzyme family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1080, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_007308_7_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P08839

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P08839

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.274.10, 1 hit
    3.20.20.60, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR008279, PEP-util_enz_mobile_dom
    IPR018274, PEP_util_AS
    IPR000121, PEP_util_C
    IPR023151, PEP_util_CS
    IPR036637, Phosphohistidine_dom_sf
    IPR024692, PTS_EI
    IPR006318, PTS_EI-like
    IPR008731, PTS_EIN
    IPR036618, PtsI_HPr-bd_sf
    IPR015813, Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442, Pyrv_Kinase-like_dom_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF05524, PEP-utilisers_N, 1 hit
    PF00391, PEP-utilizers, 1 hit
    PF02896, PEP-utilizers_C, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000732, PTS_enzyme_I, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF47831, SSF47831, 1 hit
    SSF51621, SSF51621, 1 hit
    SSF52009, SSF52009, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01417, PTS_I_fam, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00742, PEP_ENZYMES_2, 1 hit
    PS00370, PEP_ENZYMES_PHOS_SITE, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P08839-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA 
            60         70         80         90        100
    SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA 
           110        120        130        140        150
    DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS 
           160        170        180        190        200
    AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP 
           210        220        230        240        250
    AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK 
           260        270        280        290        300
    AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL 
           310        320        330        340        350
    FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE 
           360        370        380        390        400
    ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR 
           410        420        430        440        450
    ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS 
           460        470        480        490        500
    IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG 
           510        520        530        540        550
    MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE 
           560        570 
    QALAQPTTDE LMTLVNKFIE EKTIC
    Length:575
    Mass (Da):63,562
    Last modified:November 1, 1988 - 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:i4278F0838855E950
    GO

    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
    		J02796 Genomic DNA Translation: AAA24441.1
    M10425 Genomic DNA Translation: AAA24439.1
    U00096 Genomic DNA Translation: AAC75469.1
    AP009048 Genomic DNA Translation: BAA16290.1
    M21994 Genomic DNA Translation: AAA24385.1
    M21451 Genomic DNA Translation: AAA23656.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B29785, WQECPI

    NCBI Reference Sequences

    More...    RefSeqi    		NP_416911.1, NC_000913.3
    WP_000623140.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC75469; AAC75469; b2416
    BAA16290; BAA16290; BAA16290

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		57729421
    946879

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW2409
    eco:b2416

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.4315

    <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
    		J02796 Genomic DNA Translation: AAA24441.1
    M10425 Genomic DNA Translation: AAA24439.1
    U00096 Genomic DNA Translation: AAC75469.1
    AP009048 Genomic DNA Translation: BAA16290.1
    M21994 Genomic DNA Translation: AAA24385.1
    M21451 Genomic DNA Translation: AAA23656.1
    PIRiB29785, WQECPI
    RefSeqiNP_416911.1, NC_000913.3
    WP_000623140.1, 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
    1EZANMR-A1-258[»]
    1EZBNMR-A1-258[»]
    1EZCNMR-A1-258[»]
    1EZDNMR-A1-258[»]
    1ZYMX-ray2.50A/B1-258[»]
    2EZANMR-A1-258[»]
    2EZBNMR-A1-258[»]
    2EZCNMR-A1-258[»]
    2HWGX-ray2.70A/B1-575[»]
    2KX9Other-A/B1-573[»]
    2L5HOther-A/B1-573[»]
    2MP0NMR-A1-258[»]
    2N5TOther-A/B1-575[»]
    2XDFOther-A/B1-573[»]
    3EZANMR-A1-249[»]
    3EZBNMR-A1-258[»]
    3EZENMR-A1-258[»]
    6V9KX-ray1.90A/B261-575[»]
    6VU0X-ray3.50A/B261-575[»]
    BMRBiP08839
    SMRiP08839
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260570, 520 interactors
    851219, 3 interactors
    DIPiDIP-10603N
    IntActiP08839, 14 interactors
    MINTiP08839
    STRINGi511145.b2416

    Protein family/group databases

    TCDBi8.A.7.1.1, the phosphotransferase system enzyme i (ei) family

    2D gel databases

    SWISS-2DPAGEiP08839

    Proteomic databases

    jPOSTiP08839
    PaxDbiP08839
    PRIDEiP08839

    Genome annotation databases

    EnsemblBacteriaiAAC75469; AAC75469; b2416
    BAA16290; BAA16290; BAA16290
    GeneIDi57729421
    946879
    KEGGiecj:JW2409
    eco:b2416
    PATRICifig|1411691.4.peg.4315

    Organism-specific databases

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

    More...    EchoBASEi    		EB0782

    Phylogenomic databases

    eggNOGiCOG1080, Bacteria
    HOGENOMiCLU_007308_7_0_6
    InParanoidiP08839
    PhylomeDBiP08839

    Enzyme and pathway databases

    BioCyciEcoCyc:PTSI-MONOMER
    MetaCyc:PTSI-MONOMER
    BRENDAi2.7.3.9, 2026
    SABIO-RKiP08839

    Miscellaneous databases

    EvolutionaryTraceiP08839

    Protein Ontology

    More...    PROi    		PR:P08839

    Family and domain databases

    Gene3Di1.10.274.10, 1 hit
    3.20.20.60, 1 hit
    InterProiView protein in InterPro
    IPR008279, PEP-util_enz_mobile_dom
    IPR018274, PEP_util_AS
    IPR000121, PEP_util_C
    IPR023151, PEP_util_CS
    IPR036637, Phosphohistidine_dom_sf
    IPR024692, PTS_EI
    IPR006318, PTS_EI-like
    IPR008731, PTS_EIN
    IPR036618, PtsI_HPr-bd_sf
    IPR015813, Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442, Pyrv_Kinase-like_dom_sf
    PfamiView protein in Pfam
    PF05524, PEP-utilisers_N, 1 hit
    PF00391, PEP-utilizers, 1 hit
    PF02896, PEP-utilizers_C, 1 hit
    PIRSFiPIRSF000732, PTS_enzyme_I, 1 hit
    SUPFAMiSSF47831, SSF47831, 1 hit
    SSF51621, SSF51621, 1 hit
    SSF52009, SSF52009, 1 hit
    TIGRFAMsiTIGR01417, PTS_I_fam, 1 hit
    PROSITEiView protein in PROSITE
    PS00742, PEP_ENZYMES_2, 1 hit
    PS00370, PEP_ENZYMES_PHOS_SITE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiPT1_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: P08839
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: April 7, 2021
    This is version 203 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, 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
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