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UniProtKB - P08839 (PT1_ECOLI)

Entry version 207 (25 May 2022)
Sequence version 1 (01 Nov 1988)
Previous versions | rss
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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

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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P08839

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

Identification of Orthologs from Complete Genome Data

More...OMAi		CNAEWAL

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		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[»]
AlphaFoldDBiP08839
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
GeneIDi946879
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
OMAiCNAEWAL
PhylomeDBiP08839

Enzyme and pathway databases

BioCyciEcoCyc: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

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: May 25, 2022
This is version 207 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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