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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-Experimental evidence at protein leveli

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel

Keywords - Biological processi

Ion transport, Transport

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
pH-gated potassium channel KcsA
Alternative name(s):
Streptomyces lividans K+ channel
Short name:
SKC1
Gene namesi
Name:kcsA
Synonyms:skc1
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 27CytoplasmicAdd BLAST27
Transmembranei28 – 50HelicalAdd BLAST23
Topological domaini51 – 61ExtracellularAdd BLAST11
Intramembranei62 – 72Helical; Pore-formingAdd BLAST11
Intramembranei73 – 80Pore-forming8
Topological domaini81 – 87Extracellular7
Transmembranei88 – 111HelicalAdd BLAST24
Topological domaini112 – 160CytoplasmicAdd BLAST49

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells grow slower and to lower myceliar densities.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi71E → A: Prevents channel inactivation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000541021 – 160pH-gated potassium channel KcsAAdd BLAST160

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7262059,EBI-7262059

Protein-protein interaction databases

DIPiDIP-29626N.
MINTiMINT-7259978.

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 51Combined sources27
Beta strandi52 – 55Combined sources4
Helixi62 – 73Combined sources12
Beta strandi79 – 81Combined sources3
Helixi86 – 120Combined sources35
Turni121 – 123Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
1S33model-A/B/C/D23-119[»]
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-ray2.05C22-103[»]
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[»]
ProteinModelPortaliP0A334.
SMRiP0A334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A334.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi75 – 80Selectivity filter6

Domaini

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

Sequence similaritiesi

Belongs to the potassium channel family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR013099. K_chnl_dom.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF07885. Ion_trans_2. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.

Sequencei

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
Checksum:iDEBD9E64384BF40C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37969 Genomic DNA. Translation: CAA86025.1.
PIRiS60172.

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:
PDBei
RCSB PDBi
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[»]
1S33model-A/B/C/D23-119[»]
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-ray2.05C22-103[»]
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[»]
ProteinModelPortaliP0A334.
SMRiP0A334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29626N.
MINTiMINT-7259978.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0A334.

Family and domain databases

InterProiIPR013099. K_chnl_dom.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF07885. Ion_trans_2. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
ProtoNetiSearch...

Entry informationi

Entry nameiKCSA_STRLI
AccessioniPrimary (citable) accession number: P0A334
Secondary accession number(s): Q54397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 2, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.