Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P69797 (PTNAB_ECOLI)

Protein

PTS system mannose-specific EIIAB component

Gene

manX

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

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494).6 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei10Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation4 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei89Involved in the phosphoryl transfer between H-10 and H-1751 Publication1
Active sitei175Pros-phosphohistidine intermediate; for EIIB activity2 Publications1

<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 functionKinase, Transferase
Biological processPhosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

Protein family/group databases

Transport Classification Database

More...TCDBi		4.A.6.1.1 the pts mannose-fructose-sorbose (man) 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_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:
PTS system mannose-specific EIIAB component1 Publication (EC:2.7.1.1912 Publications)
Alternative name(s):
EIIAB-Man1 Publication
EIII-Man1 Publication
Including the following 2 domains:
Mannose-specific phosphotransferase enzyme IIA component1 Publication
Alternative name(s):
PTS system mannose-specific EIIA component1 Publication
Mannose-specific phosphotransferase enzyme IIB component1 Publication
Alternative name(s):
PTS system mannose-specific EIIB component1 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:manX1 Publication
Synonyms:gptB, ptsL1 Publication
Ordered Locus Names:b1817, JW1806
<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		EG10567 manX

<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 ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<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_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>Mutagenesisi10H → C: Loss of phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi10H → E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex. 1 Publication1
Mutagenesisi12W → F: Slight phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi48K → C: Retains more than 50% of phosphotransferase activity. 1 Publication1
Mutagenesisi72S → C: Slight phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi86H → N: Loss of phosphotransferase activity. 1 Publication1
Mutagenesisi110S → C: Retains more than 50% of phosphotransferase activity. 1 Publication1
Mutagenesisi175H → C: Loss of phosphotransferase activity. 1 Publication1
Mutagenesisi219H → Q: Slight phosphotransferase activity. 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 <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 Publication1 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_00001866532 – 323PTS system mannose-specific EIIAB componentAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei10Phosphohistidine; by HPr2 Publications1
Modified residuei55N6-acetyllysine1 Publication1
Modified residuei175Phosphohistidine; by EIIAPROSITE-ProRule annotation2 Publications1
Modified residuei234N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P69797

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P69797

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

More...PaxDbi		P69797

PRoteomics IDEntifications database

More...PRIDEi		P69797

2D gel databases

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

More...SWISS-2DPAGEi		P69797

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P69797

<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

Homodimer.1 Publication4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
cytRP0ACN72EBI-554089,EBI-1125696

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259144, 308 interactors
850691, 1 interactor

Database of interacting proteins

More...DIPi		DIP-35846N

Protein interaction database and analysis system

More...IntActi		P69797, 15 interactors

Molecular INTeraction database

More...MINTi		P69797

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_1955

<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

1323
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
1PDOX-ray1.70A2-133[»]
1VRCNMR-A/B1-133[»]
1VSQNMR-A/B2-134[»]
C159-323[»]
2JZHNMR-A154-323[»]
2JZNNMR-A/B2-134[»]
C159-323[»]
2JZONMR-A/B2-134[»]
D159-323[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P69797

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

More...SMRi		P69797

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		P69797

<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>Domaini2 – 124PTS EIIA type-4PROSITE-ProRule annotation2 PublicationsAdd BLAST123
Domaini157 – 320PTS EIIB type-4PROSITE-ProRule annotation1 PublicationAdd BLAST164

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>Regioni137 – 155Hinge1 PublicationAdd BLAST19

<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 PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain.2 Publications
The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain.PROSITE-ProRule annotation1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105DAS Bacteria
COG2893 LUCA
COG3444 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000140047

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P69797

KEGG Orthology (KO)

More...KOi		K02793
K02794

Database for complete collections of gene phylogenies

More...PhylomeDBi		P69797

Family and domain databases

Conserved Domains Database

More...CDDi		cd00006 PTS_IIA_man, 1 hit
cd00001 PTS_IIB_man, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.35.10, 1 hit
3.40.50.510, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013789 PTS_EIIA_man
IPR004701 PTS_EIIA_man-typ
IPR036662 PTS_EIIA_man-typ_sf
IPR033887 PTS_IIA_man
IPR004720 PTS_IIB_sorbose-sp
IPR036667 PTS_IIB_sorbose-sp_sf
IPR018455 PTS_IIB_sorbose-sp_subgr

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03610 EIIA-man, 1 hit
PF03830 PTSIIB_sorb, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52728 SSF52728, 1 hit
SSF53062 SSF53062, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00824 EIIA-man, 1 hit
TIGR00854 pts-sorbose, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51096 PTS_EIIA_TYPE_4, 1 hit
PS51101 PTS_EIIB_TYPE_4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P69797-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN 
        60         70         80         90        100
AQLAKLDTTK GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE 
       110        120        130        140        150
TLMARDDDPS FDELVALAVE TGREGVKALK AKPVEKAAPA PAAAAPKAAP 
       160        170        180        190        200
TPAKPMGPND YMVIGLARID DRLIHGQVAT RWTKETNVSR IIVVSDEVAA 
       210        220        230        240        250
DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV MLLFTNPTDV 
       260        270        280        290        300
ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE 
       310        320 
LEVRKVSTDP KLKMMDLISK IDK
Length:323
Mass (Da):35,048
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:iA446B79421B8C040
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 conflicti2 – 23TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110 (Ref. 1) CuratedAdd BLAST22
Sequence conflicti35D → N in AAA24110 (Ref. 1) Curated1
Sequence conflicti101T → R in AAA24110 (Ref. 1) Curated1
Sequence conflicti142A → G in AAA24110 (Ref. 1) Curated1

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
M36404 Genomic DNA Translation: AAA24110.1
J02699 Genomic DNA Translation: AAA24443.1
U00096 Genomic DNA Translation: AAC74887.1
AP009048 Genomic DNA Translation: BAA15624.1

Protein sequence database of the Protein Information Resource

More...PIRi		A30286 WQECM3

NCBI Reference Sequences

More...RefSeqi		NP_416331.1, NC_000913.3
WP_000150543.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74887; AAC74887; b1817
BAA15624; BAA15624; BAA15624

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946334

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1806
eco:b1817

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.434

<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
M36404 Genomic DNA Translation: AAA24110.1
J02699 Genomic DNA Translation: AAA24443.1
U00096 Genomic DNA Translation: AAC74887.1
AP009048 Genomic DNA Translation: BAA15624.1
PIRiA30286 WQECM3
RefSeqiNP_416331.1, NC_000913.3
WP_000150543.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PDOX-ray1.70A2-133[»]
1VRCNMR-A/B1-133[»]
1VSQNMR-A/B2-134[»]
C159-323[»]
2JZHNMR-A154-323[»]
2JZNNMR-A/B2-134[»]
C159-323[»]
2JZONMR-A/B2-134[»]
D159-323[»]
ProteinModelPortaliP69797
SMRiP69797
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259144, 308 interactors
850691, 1 interactor
DIPiDIP-35846N
IntActiP69797, 15 interactors
MINTiP69797
STRINGi316385.ECDH10B_1955

Protein family/group databases

TCDBi4.A.6.1.1 the pts mannose-fructose-sorbose (man) family

PTM databases

iPTMnetiP69797

2D gel databases

SWISS-2DPAGEiP69797

Proteomic databases

EPDiP69797
jPOSTiP69797
PaxDbiP69797
PRIDEiP69797

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74887; AAC74887; b1817
BAA15624; BAA15624; BAA15624
GeneIDi946334
KEGGiecj:JW1806
eco:b1817
PATRICifig|1411691.4.peg.434

Organism-specific databases

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

More...EchoBASEi		EB0562
EcoGeneiEG10567 manX

Phylogenomic databases

eggNOGiENOG4105DAS Bacteria
COG2893 LUCA
COG3444 LUCA
HOGENOMiHOG000140047
InParanoidiP69797
KOiK02793
K02794
PhylomeDBiP69797

Enzyme and pathway databases

BioCyciEcoCyc:MANX-MONOMER
MetaCyc:MANX-MONOMER

Miscellaneous databases

EvolutionaryTraceiP69797

Protein Ontology

More...PROi		PR:P69797

Family and domain databases

CDDicd00006 PTS_IIA_man, 1 hit
cd00001 PTS_IIB_man, 1 hit
Gene3Di3.40.35.10, 1 hit
3.40.50.510, 1 hit
InterProiView protein in InterPro
IPR013789 PTS_EIIA_man
IPR004701 PTS_EIIA_man-typ
IPR036662 PTS_EIIA_man-typ_sf
IPR033887 PTS_IIA_man
IPR004720 PTS_IIB_sorbose-sp
IPR036667 PTS_IIB_sorbose-sp_sf
IPR018455 PTS_IIB_sorbose-sp_subgr
PfamiView protein in Pfam
PF03610 EIIA-man, 1 hit
PF03830 PTSIIB_sorb, 1 hit
SUPFAMiSSF52728 SSF52728, 1 hit
SSF53062 SSF53062, 1 hit
TIGRFAMsiTIGR00824 EIIA-man, 1 hit
TIGR00854 pts-sorbose, 1 hit
PROSITEiView protein in PROSITE
PS51096 PTS_EIIA_TYPE_4, 1 hit
PS51101 PTS_EIIB_TYPE_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPTNAB_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: P69797
Secondary accession number(s): P08186, Q47350
<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: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 132 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again