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 - P0C0S1 (MSCS_ECOLI)

Protein

Small-conductance mechanosensitive channel

Gene

mscS

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

Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds.11 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

  • identical protein binding Source: IntAct
  • mechanosensitive ion channel activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cellular water homeostasis Source: EcoCyc
  • ion transmembrane transport Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
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 functionIon channel
Biological processIon transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11160-MONOMER

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) 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:
Small-conductance mechanosensitive channel
<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:mscS
Synonyms:yggB
Ordered Locus Names:b2924, JW2891
<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		EG11160 mscS

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 30Periplasmic1 PublicationAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei31 – 52Helical2 PublicationsAdd BLAST22
Topological domaini53 – 67Cytoplasmic1 PublicationAdd BLAST15
Transmembranei68 – 88Helical2 PublicationsAdd BLAST21
Topological domaini89 – 90Periplasmic1 Publication2
Transmembranei91 – 111Helical2 PublicationsAdd BLAST21
Topological domaini112 – 286Cytoplasmic1 PublicationAdd BLAST175

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, 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>Mutagenesisi40V → C, G or N: No detectable phenotype. 1 Publication1
Mutagenesisi40V → D or K: Normal growth stops, without cell death, due to increased membrane permeability to potassium ions and protons (permeability tested only for D substitutions). 1 Publication1
Mutagenesisi58S → C: Readily forms disulfide bonds with cross-linkers, suggesting that individual S-58 are only 3 Angstroms apart in the closed state, versus 33 Angstroms apart in the open state crystal structure. 1 Publication1
Mutagenesisi158A → F: Decreased conductance, due to decreased diameter of the channel portal. 1 Publication1
Mutagenesisi266 – 286ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 1 PublicationAdd BLAST21
Mutagenesisi266 – 286ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. 1 PublicationAdd BLAST21
Mutagenesisi267S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001102381 – 286Small-conductance mechanosensitive channelAdd BLAST286

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0C0S1

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

More...PaxDbi		P0C0S1

PRoteomics IDEntifications database

More...PRIDEi		P0C0S1

<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

Homoheptamer.7 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
itself5EBI-554616,EBI-554616

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259238, 255 interactors

Database of interacting proteins

More...DIPi		DIP-36192N

Protein interaction database and analysis system

More...IntActi		P0C0S1, 2 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_3099

<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

1286
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
2OAUX-ray3.70A/B/C/D/E/F/G1-286[»]
2VV5X-ray3.45A/B/C/D/E/F/G1-286[»]
3UDCX-ray3.36A/B/C/D/E/F/G272-286[»]
4AGEX-ray4.84A/B/C/D/E/F/G1-286[»]
4AGFX-ray4.70A/B/C/D/E/F/G1-286[»]
4HWAX-ray4.37A/B/C/D/E/F/G1-286[»]
5AJIX-ray2.99A/B/C/D/E/F/G1-286[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0C0S1

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

More...SMRi		P0C0S1

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		P0C0S1

<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

<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 channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus, and is probably influenced by freely exchangeable membrane lipids that bind in grooves and pockets between the transmembrane helices and enhance the stability of the closed channel conformation. In a hypoosmotic environment the membrane is stretched, and lipids may be pulled into the lipid bilayer and away from the protein, which is predicted to destabilize the closed conformation and promote channel gating.5 Publications

<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 MscS (TC 1.A.23) family. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105D64 Bacteria
COG0668 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000110050

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0C0S1

KEGG Orthology (KO)

More...KOi		K03442

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0C0S1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR010920 LSM_dom_sf
IPR011066 MscC_channel_C
IPR006685 MscS_channel
IPR006686 MscS_channel_CS
IPR011014 MscS_channel_TM-2
IPR023408 MscS_dom_sf
IPR008910 TM_helix

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00924 MS_channel, 1 hit
PF05552 TM_helix, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50182 SSF50182, 1 hit
SSF82689 SSF82689, 1 hit
SSF82861 SSF82861, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01246 UPF0003, 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.

P0C0S1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN 
        60         70         80         90        100
AVNRLMISRK IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL 
       110        120        130        140        150
GAAGLAVGLA LQGSLSNLAA GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI 
       160        170        180        190        200
FSTTMRTADG KIIVIPNGKI IAGNIINFSR EPVRRNEFII GVAYDSDIDQ 
       210        220        230        240        250
VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW SNSGDLQNVY 
       260        270        280 
WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA
Length:286
Mass (Da):30,896
Last modified:December 6, 2005 - 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:iFF00AD64F795E9FE
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
X14436 Genomic DNA Translation: CAA32606.1
U28377 Genomic DNA Translation: AAA69091.1
U00096 Genomic DNA Translation: AAC75961.1
AP009048 Genomic DNA Translation: BAE76988.1

Protein sequence database of the Protein Information Resource

More...PIRi		S04735 QQEC4A

NCBI Reference Sequences

More...RefSeqi		NP_417399.1, NC_000913.3
WP_000389818.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75961; AAC75961; b2924
BAE76988; BAE76988; BAE76988

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947416

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2891
eco:b2924

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3808

<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
X14436 Genomic DNA Translation: CAA32606.1
U28377 Genomic DNA Translation: AAA69091.1
U00096 Genomic DNA Translation: AAC75961.1
AP009048 Genomic DNA Translation: BAE76988.1
PIRiS04735 QQEC4A
RefSeqiNP_417399.1, NC_000913.3
WP_000389818.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OAUX-ray3.70A/B/C/D/E/F/G1-286[»]
2VV5X-ray3.45A/B/C/D/E/F/G1-286[»]
3UDCX-ray3.36A/B/C/D/E/F/G272-286[»]
4AGEX-ray4.84A/B/C/D/E/F/G1-286[»]
4AGFX-ray4.70A/B/C/D/E/F/G1-286[»]
4HWAX-ray4.37A/B/C/D/E/F/G1-286[»]
5AJIX-ray2.99A/B/C/D/E/F/G1-286[»]
ProteinModelPortaliP0C0S1
SMRiP0C0S1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259238, 255 interactors
DIPiDIP-36192N
IntActiP0C0S1, 2 interactors
STRINGi316385.ECDH10B_3099

Protein family/group databases

TCDBi1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family

Proteomic databases

jPOSTiP0C0S1
PaxDbiP0C0S1
PRIDEiP0C0S1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75961; AAC75961; b2924
BAE76988; BAE76988; BAE76988
GeneIDi947416
KEGGiecj:JW2891
eco:b2924
PATRICifig|1411691.4.peg.3808

Organism-specific databases

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

More...EchoBASEi		EB1149
EcoGeneiEG11160 mscS

Phylogenomic databases

eggNOGiENOG4105D64 Bacteria
COG0668 LUCA
HOGENOMiHOG000110050
InParanoidiP0C0S1
KOiK03442
PhylomeDBiP0C0S1

Enzyme and pathway databases

BioCyciEcoCyc:EG11160-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0C0S1

Protein Ontology

More...PROi		PR:P0C0S1

Family and domain databases

Gene3Di2.30.30.60, 1 hit
InterProiView protein in InterPro
IPR010920 LSM_dom_sf
IPR011066 MscC_channel_C
IPR006685 MscS_channel
IPR006686 MscS_channel_CS
IPR011014 MscS_channel_TM-2
IPR023408 MscS_dom_sf
IPR008910 TM_helix
PfamiView protein in Pfam
PF00924 MS_channel, 1 hit
PF05552 TM_helix, 1 hit
SUPFAMiSSF50182 SSF50182, 1 hit
SSF82689 SSF82689, 1 hit
SSF82861 SSF82861, 1 hit
PROSITEiView protein in PROSITE
PS01246 UPF0003, 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 nameiMSCS_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: P0C0S1
Secondary accession number(s): P11666, Q2M9R8
<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: December 6, 2005
Last sequence update: December 6, 2005
Last modified: January 16, 2019
This is version 118 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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