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UniProtKB - P0A334 (KCSA_STRLI)

Entry version 87 (25 May 2022)
Sequence version 1 (15 Mar 2005)
Previous versions | rss
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Protein

pH-gated potassium channel KcsA

Gene

kcsA

Organism
Streptomyces lividans
Status
Reviewed-Annotation score:

Annotation score:4 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

Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K+ > Rb+ > NH4+ >> Na+ > Li+.

1 Publication

Miscellaneous

The amino acids 62-79 are situated in the membrane and are important for channel structure and properties.

<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 ...

<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, Ligand-gated ion channel
Biological processIon transport, Transport

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.1.1.1, the voltage-gated ion channel (vic) superfamily

<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:
pH-gated potassium channel KcsA
Alternative name(s):
Streptomyces lividans K+ channel
Short name:
SKC1
<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:kcsA
Synonyms:skc1
<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>OrganismiStreptomyces lividans
<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 identifieri1916 [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 › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces

<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%5Flocation%5Fsection">'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 – 27CytoplasmicAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei28 – 50HelicalAdd BLAST23
Topological domaini51 – 61ExtracellularAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei62 – 72Helical; Pore-formingAdd BLAST11
Intramembranei73 – 80Pore-forming8
Topological domaini81 – 87Extracellular7
Transmembranei88 – 111HelicalAdd BLAST24
Topological domaini112 – 160CytoplasmicAdd BLAST49

Keywords - Cellular componenti

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells grow slower and to lower myceliar densities.1 Publication

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>Mutagenesisi71E → A: Prevents channel inactivation. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB07416, (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE
DB01851, Tetrabutylammonium Ion
DB08837, Tetraethylammonium

<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_00000541021 – 160pH-gated potassium channel KcsAAdd BLAST160

<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

Homotetramer.

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

P0A334
With#Exp.IntAct
itself37EBI-7262059,EBI-7262059

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-29626N

Molecular INTeraction database

More...MINTi		P0A334

<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

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P0A334

Biological Magnetic Resonance Data Bank

More...BMRBi		P0A334

The Protein Circular Dichroism Data Bank

More...PCDDBi		P0A334

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

More...SMRi		P0A334

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		P0A334

<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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi75 – 80Selectivity filter6

<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 cytoplasmic C-terminus is involved in the gating mechanism.

<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 potassium channel family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013099, K_chnl_dom
IPR028325, VG_K_chnl

The PANTHER Classification System

More...PANTHERi		PTHR11537, PTHR11537, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07885, Ion_trans_2, 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.

P0A334-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPMLSGLLA RLVKLLLGRH GSALHWRAAG AATVLLVIVL LAGSYLAVLA 
        60         70         80         90        100
ERGAPGAQLI TYPRALWWSV ETATTVGYGD LYPVTLWGRL VAVVVMVAGI 
       110        120        130        140        150
TSFGLVTAAL ATWFVGREQE RRGHFVRHSE KAAEEAYTRT TRALHERFDR 
       160
LERMLDDNRR
Length:160
Mass (Da):17,694
Last modified:March 15, 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:iDEBD9E64384BF40C
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
Z37969 Genomic DNA Translation: CAA86025.1

Protein sequence database of the Protein Information Resource

More...PIRi		S60172

<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
Z37969 Genomic DNA Translation: CAA86025.1
PIRiS60172

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
1BL8X-ray3.20A/B/C/D23-119[»]
1F6GNMR-A/B/C/D1-160[»]
1J95X-ray2.80A/B/C/D1-125[»]
1JQ1NMR-A/B/C/D86-119[»]
1JQ2NMR-A/B/C/D86-119[»]
1JVMX-ray2.80A/B/C/D1-125[»]
1K4CX-ray2.00C1-124[»]
1K4DX-ray2.30C1-124[»]
1R3IX-ray2.40C1-124[»]
1R3JX-ray1.90C1-124[»]
1R3KX-ray2.80C1-124[»]
1R3LX-ray2.41C1-124[»]
1ZWIX-ray2.50C22-123[»]
2A9HNMR-A/B/C/D1-132[»]
2ATKX-ray2.50C1-124[»]
2BOBX-ray2.76C1-124[»]
2BOCX-ray3.01C1-124[»]
2DWDX-ray2.60C22-124[»]
2DWEX-ray2.50C22-124[»]
2H8PX-ray2.25C22-78[»]
D80-122[»]
2HG5X-ray2.75C22-78[»]
D80-122[»]
2HJFX-ray2.90C22-124[»]
2HVJX-ray2.75C1-124[»]
2HVKX-ray1.90C1-124[»]
2IH1X-ray2.40C3-122[»]
2IH3X-ray1.72C3-122[»]
2ITCX-ray3.20C1-124[»]
2ITDX-ray2.70C1-124[»]
2JK5X-ray2.40C1-124[»]
2NLJX-ray2.52C1-124[»]
2P7TX-ray2.05C22-124[»]
2QTOX-ray3.20A/B/C/D23-119[»]
2W0FX-ray2.40C1-124[»]
3EFFX-ray3.80K/L/M/N22-160[»]
3F5WX-ray3.30C21-124[»]
3F7VX-ray3.20C21-124[»]
3F7YX-ray3.40C21-124[»]
3FB5X-ray2.80C21-124[»]
3FB6X-ray3.00C21-124[»]
3FB7X-ray3.30C21-124[»]
3FB8X-ray3.40C21-124[»]
3GB7X-ray2.85C1-124[»]
3HPLX-ray3.20C1-124[»]
3IFXOther3.56A/B/C/D1-123[»]
3IGAX-ray2.75C1-124[»]
3OGCX-ray3.80C2-124[»]
3OR6X-ray2.70C22-124[»]
3OR7X-ray2.30C22-124[»]
3PJSX-ray3.80K/L/M/N22-160[»]
3STLX-ray2.40C22-124[»]
3STZX-ray2.50C23-124[»]
4LBEX-ray2.75C2-124[»]
4LCUX-ray2.75C2-124[»]
4MSWX-ray2.06C22-124[»]
4UUJX-ray2.40C22-124[»]
5E1AX-ray3.40C4-124[»]
5EBLX-ray2.30C1-125[»]
5EBMX-ray2.50C1-125[»]
5EBWX-ray2.30C1-123[»]
5EC1X-ray2.75C1-125[»]
5EC2X-ray2.30C1-125[»]
5J9PX-ray2.85C22-117[»]
5VK6X-ray2.25C26-121[»]
5VKEX-ray2.37C26-121[»]
5VKHX-ray2.25C22-124[»]
6NFUX-ray2.09C22-124[»]
6NFVX-ray2.13C22-124[»]
6PA0X-ray2.05C22-124[»]
6W0AX-ray3.24C28-120[»]
6W0BX-ray3.60C28-120[»]
6W0CX-ray3.56C28-120[»]
6W0DX-ray3.64C28-120[»]
6W0EX-ray3.51C28-120[»]
6W0FX-ray2.40C22-124[»]
6W0GX-ray2.60C22-124[»]
6W0HX-ray2.60C22-124[»]
6W0IX-ray2.33C22-124[»]
6W0JX-ray2.50C22-124[»]
7M2IX-ray2.69C26-116[»]
7M2JX-ray3.20C26-116[»]
7RP0X-ray2.48C22-124[»]
AlphaFoldDBiP0A334
BMRBiP0A334
PCDDBiP0A334
SMRiP0A334
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-29626N
MINTiP0A334

Chemistry databases

DrugBankiDB07416, (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE
DB01851, Tetrabutylammonium Ion
DB08837, Tetraethylammonium

Protein family/group databases

TCDBi1.A.1.1.1, the voltage-gated ion channel (vic) superfamily

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P0A334, 3 sequenced antibodies

Miscellaneous databases

EvolutionaryTraceiP0A334

Family and domain databases

InterProiView protein in InterPro
IPR013099, K_chnl_dom
IPR028325, VG_K_chnl
PANTHERiPTHR11537, PTHR11537, 1 hit
PfamiView protein in Pfam
PF07885, Ion_trans_2, 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 nameiKCSA_STRLI
<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: P0A334
Secondary accession number(s): Q54397
<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: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 25, 2022
This is version 87 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

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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