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P0A334

- KCSA_STRLI

UniProt

P0A334 - KCSA_STRLI

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Protein

pH-gated potassium channel KcsA

Gene

kcsA

Organism
Streptomyces lividans
Status
Reviewed - 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

  1. identical protein binding Source: IntAct
  2. voltage-gated potassium channel activity Source: InterPro
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. voltage-gated potassium channel complex Source: InterPro
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711E → A: Prevents channel inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160pH-gated potassium channel KcsAPRO_0000054102Add
BLAST

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

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 5127
Beta strandi52 – 554
Helixi62 – 7312
Beta strandi79 – 813
Helixi86 – 12035
Turni121 – 1233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A334.
SMRiP0A334. Positions 22-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A334.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727CytoplasmicAdd
BLAST
Topological domaini51 – 6111ExtracellularAdd
BLAST
Topological domaini81 – 877Extracellular
Topological domaini112 – 16049CytoplasmicAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei62 – 7211Helical; Pore-formingAdd
BLAST
Intramembranei73 – 808Pore-forming

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei28 – 5023HelicalAdd
BLAST
Transmembranei88 – 11124HelicalAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi75 – 806Selectivity filter

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. 2pore_dom_K_chnl_dom.
IPR003091. K_chnl.
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 [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:
EMBL
GenBank
DDBJ
Links Updated
Z37969 Genomic DNA. Translation: CAA86025.1.
PIRiS60172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z37969 Genomic DNA. Translation: CAA86025.1 .
PIRi S60172.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BL8 X-ray 3.20 A/B/C/D 23-119 [» ]
1F6G NMR - A/B/C/D 1-160 [» ]
1J95 X-ray 2.80 A/B/C/D 1-125 [» ]
1JQ1 NMR - A/B/C/D 86-119 [» ]
1JQ2 NMR - A/B/C/D 86-119 [» ]
1JVM X-ray 2.80 A/B/C/D 1-125 [» ]
1K4C X-ray 2.00 C 1-124 [» ]
1K4D X-ray 2.30 C 1-124 [» ]
1R3I X-ray 2.40 C 1-124 [» ]
1R3J X-ray 1.90 C 1-124 [» ]
1R3K X-ray 2.80 C 1-124 [» ]
1R3L X-ray 2.41 C 1-124 [» ]
1S33 model - A/B/C/D 23-119 [» ]
1ZWI X-ray 2.50 C 22-123 [» ]
2A9H NMR - A/B/C/D 1-132 [» ]
2ATK X-ray 2.50 C 1-124 [» ]
2BOB X-ray 2.76 C 1-124 [» ]
2BOC X-ray 3.01 C 1-124 [» ]
2DWD X-ray 2.60 C 22-124 [» ]
2DWE X-ray 2.50 C 22-124 [» ]
2H8P X-ray 2.25 C 22-78 [» ]
D 80-122 [» ]
2HG5 X-ray 2.75 C 22-78 [» ]
D 80-122 [» ]
2HJF X-ray 2.90 C 22-124 [» ]
2HVJ X-ray 2.75 C 1-124 [» ]
2HVK X-ray 1.90 C 1-124 [» ]
2IH1 X-ray 2.40 C 3-122 [» ]
2IH3 X-ray 1.72 C 3-122 [» ]
2ITC X-ray 3.20 C 1-124 [» ]
2ITD X-ray 2.70 C 1-124 [» ]
2JK5 X-ray 2.40 C 1-124 [» ]
2NLJ X-ray 2.52 C 1-124 [» ]
2P7T X-ray 2.05 C 22-103 [» ]
2QTO X-ray 3.20 A/B/C/D 23-119 [» ]
2W0F X-ray 2.40 C 1-124 [» ]
3EFF X-ray 3.80 K/L/M/N 22-160 [» ]
3F5W X-ray 3.30 C 21-124 [» ]
3F7V X-ray 3.20 C 21-124 [» ]
3F7Y X-ray 3.40 C 21-124 [» ]
3FB5 X-ray 2.80 C 21-124 [» ]
3FB6 X-ray 3.00 C 21-124 [» ]
3FB7 X-ray 3.30 C 21-124 [» ]
3FB8 X-ray 3.40 C 21-124 [» ]
3GB7 X-ray 2.85 C 1-124 [» ]
3HPL X-ray 3.20 C 1-124 [» ]
3IFX Other 3.56 A/B/C/D 1-123 [» ]
3IGA X-ray 2.75 C 1-124 [» ]
3OGC X-ray 3.80 C 2-124 [» ]
3OR6 X-ray 2.70 C 22-124 [» ]
3OR7 X-ray 2.30 C 22-124 [» ]
3PJS X-ray 3.80 K/L/M/N 22-160 [» ]
3STL X-ray 2.40 C 22-124 [» ]
3STZ X-ray 2.50 C 23-124 [» ]
4LBE X-ray 2.75 C 2-124 [» ]
4LCU X-ray 2.75 C 2-124 [» ]
4MSW X-ray 2.06 C 22-124 [» ]
4UUJ X-ray 2.40 C 22-124 [» ]
ProteinModelPortali P0A334.
SMRi P0A334. Positions 22-124.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29626N.
MINTi MINT-7259978.

Protein family/group databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0A334.

Family and domain databases

InterProi IPR013099. 2pore_dom_K_chnl_dom.
IPR003091. K_chnl.
IPR028325. VG_K_chnl.
[Graphical view ]
PANTHERi PTHR11537. PTHR11537. 1 hit.
Pfami PF07885. Ion_trans_2. 1 hit.
[Graphical view ]
PRINTSi PR00169. KCHANNEL.
ProtoNeti Search...

Publicationsi

  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. Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-160 IN THE CLOSED CONFORMATION.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 2-160 IN THE OPEN CONFIGURATION.

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: October 29, 2014
This is version 61 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

External Data

Dasty 3