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P0A334 (KCSA_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
pH-gated potassium channel KcsA
Alternative name(s):
Streptomyces lividans K+ channel
Short name=SKC1
Gene names
Name:kcsA
Synonyms:skc1
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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+. Ref.1

Subunit structure

Homotetramer. Ref.6 Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein.

Domain

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

Disruption phenotype

Cells grow slower and to lower myceliar densities. Ref.1

Miscellaneous

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

Sequence similarities

Belongs to the potassium channel family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7262059,EBI-7262059

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160pH-gated potassium channel KcsA
PRO_0000054102

Regions

Topological domain1 – 2727Cytoplasmic Ref.2
Transmembrane28 – 5023Helical
Topological domain51 – 6111Extracellular Ref.2
Intramembrane62 – 7211Helical; Pore-forming
Intramembrane73 – 808Pore-forming
Topological domain81 – 877Extracellular Ref.2
Transmembrane88 – 11124Helical
Topological domain112 – 16049Cytoplasmic Ref.2
Motif75 – 806Selectivity filter

Experimental info

Mutagenesis711E → A: Prevents channel inactivation. Ref.4

Secondary structure

........... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A334 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: DEBD9E64384BF40C

FASTA16017,694
        10         20         30         40         50         60 
MPPMLSGLLA RLVKLLLGRH GSALHWRAAG AATVLLVIVL LAGSYLAVLA ERGAPGAQLI 

        70         80         90        100        110        120 
TYPRALWWSV ETATTVGYGD LYPVTLWGRL VAVVVMVAGI TSFGLVTAAL ATWFVGREQE 

       130        140        150        160 
RRGHFVRHSE KAAEEAYTRT TRALHERFDR LERMLDDNRR 

« Hide

References

[1]"A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans."
Schrempf H., Schmidt O., Kuemmerlen R., Hinnah S., Mueller D., Betzler M., Steinkamp T., Wagner R.
EMBO J. 14:5170-5178(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A K(+) CHANNEL, DISRUPTION PHENOTYPE.
Strain: 66 / 1326.
[2]"pH-dependent gating in the Streptomyces lividans K+ channel."
Cuello L.G., Romero J.G., Cortes D.M., Perozo E.
Biochemistry 37:3229-3236(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PH-GATING, SUBSTRATE SPECIFICITY, POSSIBLE TOPOLOGY.
[3]"Proteomics on full-length membrane proteins using mass spectrometry."
le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., Kaback H.R., Faull K.F.
Biochemistry 39:4237-4242(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[4]"Rearrangements in the KcsA cytoplasmic domain underlie its gating."
Hirano M., Takeuchi Y., Aoki T., Yanagida T., Ide T.
J. Biol. Chem. 285:3777-3783(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GATING MECHANISM, MUTAGENESIS OF GLU-71.
[5]"Single potassium ion seeks open channel for transmembrane travels: tales from the KcsA structure."
Gouaux E.
Structure 6:1221-1226(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"The structure of the potassium channel: molecular basis of K+ conduction and selectivity."
Doyle D.A., Morais Cabral J., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., McKinnon R.
Science 280:69-77(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), SUBUNIT.
[7]"Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating."
Cortes D.M., Cuello L.G., Perozo E.
J. Gen. Physiol. 117:165-180(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-160, EPR SPECTROSCOPY.
[8]"Structure of the KcsA channel intracellular gate in the open state."
Liu Y.-S., Sompornpisut P., Perozo E.
Nat. Struct. Biol. 8:883-887(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 86-119, EPR SPECTROSCOPY.
[9]"Energetic optimization of ion conduction rate by the K+ selectivity filter."
Morais-Cabral J.H., Zhou Y., MacKinnon R.
Nature 414:37-42(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-124, TETRAMERIZATION, POTASSIUM-BINDING.
[10]"Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution."
Zhou Y., Morais-Cabral J.H., Kaufman A., MacKinnon R.
Nature 414:43-48(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-124 IN COMPLEX WITH ANTIBODY, POTASSIUM-BINDING, TETRAMERIZATION.
[11]"Crystal structure of full-length KcsA in its closed conformation."
Uysal S., Vasquez V., Tereshko V., Esaki K., Fellouse F.A., Sidhu S.S., Koide S., Perozo E., Kossiakoff A.
Proc. Natl. Acad. Sci. U.S.A. 106:6644-6649(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-160 IN THE CLOSED CONFORMATION.
[12]"Mechanism of activation gating in the full-length KcsA K+ channel."
Uysal S., Cuello L.G., Cortes D.M., Koide S., Kossiakoff A.A., Perozo E.
Proc. Natl. Acad. Sci. U.S.A. 108:11896-11899(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 2-160 IN THE OPEN CONFIGURATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z37969 Genomic DNA. Translation: CAA86025.1.
PIRS60172.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D3-125[»]
1K4CX-ray2.00C3-124[»]
1K4DX-ray2.30C3-124[»]
1R3IX-ray2.40C3-124[»]
1R3JX-ray1.90C3-124[»]
1R3KX-ray2.80C3-124[»]
1R3LX-ray2.41C3-124[»]
1S33model-A/B/C/D23-119[»]
1ZWIX-ray2.50C22-123[»]
2A9HNMR-A/B/C/D1-132[»]
2ATKX-ray2.50C3-124[»]
2BOBX-ray2.76C3-124[»]
2BOCX-ray3.01C3-124[»]
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-ray2.75C3-124[»]
2HVKX-ray1.90C3-124[»]
2IH1X-ray2.40C3-122[»]
2IH3X-ray1.72C3-122[»]
2ITCX-ray3.20C3-124[»]
2ITDX-ray2.70C3-124[»]
2JK5X-ray2.40C1-124[»]
2NLJX-ray2.52C3-124[»]
2P7TX-ray2.05C22-124[»]
2QTOX-ray3.20A/B/C/D23-119[»]
2W0FX-ray2.40C1-124[»]
3EFFX-ray3.80K/L/M/N22-160[»]
3F5WX-ray3.30C21-119[»]
3F7VX-ray3.20C21-119[»]
3F7YX-ray3.40C21-119[»]
3FB5X-ray2.80C21-119[»]
3FB6X-ray3.00C21-119[»]
3FB7X-ray3.30C21-119[»]
3FB8X-ray3.40C21-119[»]
3GB7X-ray2.85C3-124[»]
3HPLX-ray3.20C3-124[»]
3IFXX-ray3.56A/B/C/D1-124[»]
3IGAX-ray2.75C3-124[»]
3OGCX-ray3.80C2-124[»]
3OR6X-ray2.70C22-124[»]
3OR7X-ray2.30C22-124[»]
3PJSX-ray3.80K/L/M/N2-160[»]
3STLX-ray2.40C22-124[»]
3STZX-ray2.50C23-124[»]
4LBEX-ray2.75C2-124[»]
4LCUX-ray2.75C2-124[»]
4MSWX-ray2.06C22-124[»]
ProteinModelPortalP0A334.
SMRP0A334. Positions 22-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29626N.
MINTMINT-7259978.

Protein family/group databases

TCDB1.A.1.1.1. the voltage-gated ion channel (vic) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013099. 2pore_dom_K_chnl_dom.
IPR003091. K_chnl.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF07885. Ion_trans_2. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
ProtoNetSearch...

Other

EvolutionaryTraceP0A334.

Entry information

Entry nameKCSA_STRLI
AccessionPrimary (citable) accession number: P0A334
Secondary accession number(s): Q54397
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references