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P0A334

- KCSA_STRLI

UniProt

P0A334 - KCSA_STRLI

Protein

pH-gated potassium channel KcsA

Gene

kcsA

Organism
Streptomyces lividans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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[»]
    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.

    P0A334-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPMLSGLLA RLVKLLLGRH GSALHWRAAG AATVLLVIVL LAGSYLAVLA    50
    ERGAPGAQLI TYPRALWWSV ETATTVGYGD LYPVTLWGRL VAVVVMVAGI 100
    TSFGLVTAAL ATWFVGREQE RRGHFVRHSE KAAEEAYTRT TRALHERFDR 150
    LERMLDDNRR 160
    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 [» ]
    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 1, 2014
    This is version 60 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