KCSA_STRLI
ID KCSA_STRLI Reviewed; 160 AA.
AC P0A334; Q54397;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=pH-gated potassium channel KcsA;
DE AltName: Full=Streptomyces lividans K+ channel;
DE Short=SKC1;
GN Name=kcsA; Synonyms=skc1;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A K(+) CHANNEL, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=66 / 1326;
RX PubMed=7489706; DOI=10.1002/j.1460-2075.1995.tb00201.x;
RA Schrempf H., Schmidt O., Kuemmerlen R., Hinnah S., Mueller D., Betzler M.,
RA Steinkamp T., Wagner R.;
RT "A prokaryotic potassium ion channel with two predicted transmembrane
RT segments from Streptomyces lividans.";
RL EMBO J. 14:5170-5178(1995).
RN [2]
RP PH-GATING, SUBSTRATE SPECIFICITY, AND POSSIBLE TOPOLOGY.
RX PubMed=9536962; DOI=10.1021/bi972997x;
RA Cuello L.G., Romero J.G., Cortes D.M., Perozo E.;
RT "pH-dependent gating in the Streptomyces lividans K+ channel.";
RL Biochemistry 37:3229-3236(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10757971; DOI=10.1021/bi000150m;
RA le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., Kaback H.R.,
RA Faull K.F.;
RT "Proteomics on full-length membrane proteins using mass spectrometry.";
RL Biochemistry 39:4237-4242(2000).
RN [4]
RP GATING MECHANISM, AND MUTAGENESIS OF GLU-71.
RX PubMed=19959477; DOI=10.1074/jbc.m109.084368;
RA Hirano M., Takeuchi Y., Aoki T., Yanagida T., Ide T.;
RT "Rearrangements in the KcsA cytoplasmic domain underlie its gating.";
RL J. Biol. Chem. 285:3777-3783(2010).
RN [5]
RP REVIEW.
RX PubMed=9782060; DOI=10.1016/s0969-2126(98)00122-1;
RA Gouaux E.;
RT "Single potassium ion seeks open channel for transmembrane travels: tales
RT from the KcsA structure.";
RL Structure 6:1221-1226(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=9525859; DOI=10.1126/science.280.5360.69;
RA Doyle D.A., Morais Cabral J., Pfuetzner R.A., Kuo A., Gulbis J.M.,
RA Cohen S.L., Chait B.T., McKinnon R.;
RT "The structure of the potassium channel: molecular basis of K+ conduction
RT and selectivity.";
RL Science 280:69-77(1998).
RN [7]
RP STRUCTURE BY NMR OF 1-160, AND EPR SPECTROSCOPY.
RX PubMed=11158168; DOI=10.1085/jgp.117.2.165;
RA Cortes D.M., Cuello L.G., Perozo E.;
RT "Molecular architecture of full-length KcsA: role of cytoplasmic domains in
RT ion permeation and activation gating.";
RL J. Gen. Physiol. 117:165-180(2001).
RN [8]
RP STRUCTURE BY NMR OF 86-119, AND EPR SPECTROSCOPY.
RX PubMed=11573095; DOI=10.1038/nsb1001-883;
RA Liu Y.-S., Sompornpisut P., Perozo E.;
RT "Structure of the KcsA channel intracellular gate in the open state.";
RL Nat. Struct. Biol. 8:883-887(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-124, TETRAMERIZATION, AND
RP POTASSIUM-BINDING.
RX PubMed=11689935; DOI=10.1038/35102000;
RA Morais-Cabral J.H., Zhou Y., MacKinnon R.;
RT "Energetic optimization of ion conduction rate by the K+ selectivity
RT filter.";
RL Nature 414:37-42(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-124 IN COMPLEX WITH ANTIBODY,
RP POTASSIUM-BINDING, AND TETRAMERIZATION.
RX PubMed=11689936; DOI=10.1038/35102009;
RA Zhou Y., Morais-Cabral J.H., Kaufman A., MacKinnon R.;
RT "Chemistry of ion coordination and hydration revealed by a K+ channel-Fab
RT complex at 2.0 A resolution.";
RL Nature 414:43-48(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-160 IN THE CLOSED CONFORMATION.
RX PubMed=19346472; DOI=10.1073/pnas.0810663106;
RA Uysal S., Vasquez V., Tereshko V., Esaki K., Fellouse F.A., Sidhu S.S.,
RA Koide S., Perozo E., Kossiakoff A.;
RT "Crystal structure of full-length KcsA in its closed conformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6644-6649(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 2-160 IN THE OPEN CONFIGURATION.
RX PubMed=21730186; DOI=10.1073/pnas.1105112108;
RA Uysal S., Cuello L.G., Cortes D.M., Koide S., Kossiakoff A.A., Perozo E.;
RT "Mechanism of activation gating in the full-length KcsA K+ channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11896-11899(2011).
CC -!- FUNCTION: Acts as a pH-gated potassium ion channel; changing the
CC cytosolic pH from 7 to 4 opens the channel, although it is not clear if
CC this is the physiological stimulus for channel opening. Monovalent
CC cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).
CC {ECO:0000269|PubMed:7489706}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11689936,
CC ECO:0000269|PubMed:9525859}.
CC -!- INTERACTION:
CC P0A334; P0A334: kcsA; NbExp=37; IntAct=EBI-7262059, EBI-7262059;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The cytoplasmic C-terminus is involved in the gating mechanism.
CC -!- DISRUPTION PHENOTYPE: Cells grow slower and to lower myceliar
CC densities. {ECO:0000269|PubMed:7489706}.
CC -!- MISCELLANEOUS: The amino acids 62-79 are situated in the membrane and
CC are important for channel structure and properties.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; Z37969; CAA86025.1; -; Genomic_DNA.
DR PIR; S60172; S60172.
DR PDB; 1BL8; X-ray; 3.20 A; A/B/C/D=23-119.
DR PDB; 1F6G; NMR; -; A/B/C/D=1-160.
DR PDB; 1J95; X-ray; 2.80 A; A/B/C/D=1-125.
DR PDB; 1JQ1; NMR; -; A/B/C/D=86-119.
DR PDB; 1JQ2; NMR; -; A/B/C/D=86-119.
DR PDB; 1JVM; X-ray; 2.80 A; A/B/C/D=1-125.
DR PDB; 1K4C; X-ray; 2.00 A; C=1-124.
DR PDB; 1K4D; X-ray; 2.30 A; C=1-124.
DR PDB; 1R3I; X-ray; 2.40 A; C=1-124.
DR PDB; 1R3J; X-ray; 1.90 A; C=1-124.
DR PDB; 1R3K; X-ray; 2.80 A; C=1-124.
DR PDB; 1R3L; X-ray; 2.41 A; C=1-124.
DR PDB; 1ZWI; X-ray; 2.50 A; C=22-123.
DR PDB; 2A9H; NMR; -; A/B/C/D=1-132.
DR PDB; 2ATK; X-ray; 2.50 A; C=1-124.
DR PDB; 2BOB; X-ray; 2.76 A; C=1-124.
DR PDB; 2BOC; X-ray; 3.01 A; C=1-124.
DR PDB; 2DWD; X-ray; 2.60 A; C=22-124.
DR PDB; 2DWE; X-ray; 2.50 A; C=22-124.
DR PDB; 2H8P; X-ray; 2.25 A; C=22-78, D=80-122.
DR PDB; 2HG5; X-ray; 2.75 A; C=22-78, D=80-122.
DR PDB; 2HJF; X-ray; 2.90 A; C=22-124.
DR PDB; 2HVJ; X-ray; 2.75 A; C=1-124.
DR PDB; 2HVK; X-ray; 1.90 A; C=1-124.
DR PDB; 2IH1; X-ray; 2.40 A; C=3-122.
DR PDB; 2IH3; X-ray; 1.72 A; C=3-122.
DR PDB; 2ITC; X-ray; 3.20 A; C=1-124.
DR PDB; 2ITD; X-ray; 2.70 A; C=1-124.
DR PDB; 2JK5; X-ray; 2.40 A; C=1-124.
DR PDB; 2NLJ; X-ray; 2.52 A; C=1-124.
DR PDB; 2P7T; X-ray; 2.05 A; C=22-124.
DR PDB; 2QTO; X-ray; 3.20 A; A/B/C/D=23-119.
DR PDB; 2W0F; X-ray; 2.40 A; C=1-124.
DR PDB; 3EFF; X-ray; 3.80 A; K/L/M/N=22-160.
DR PDB; 3F5W; X-ray; 3.30 A; C=21-124.
DR PDB; 3F7V; X-ray; 3.20 A; C=21-124.
DR PDB; 3F7Y; X-ray; 3.40 A; C=21-124.
DR PDB; 3FB5; X-ray; 2.80 A; C=21-124.
DR PDB; 3FB6; X-ray; 3.00 A; C=21-124.
DR PDB; 3FB7; X-ray; 3.30 A; C=21-124.
DR PDB; 3FB8; X-ray; 3.40 A; C=21-124.
DR PDB; 3GB7; X-ray; 2.85 A; C=1-124.
DR PDB; 3HPL; X-ray; 3.20 A; C=1-124.
DR PDB; 3IFX; Other; 3.56 A; A/B/C/D=1-123.
DR PDB; 3IGA; X-ray; 2.75 A; C=1-124.
DR PDB; 3OGC; X-ray; 3.80 A; C=2-124.
DR PDB; 3OR6; X-ray; 2.70 A; C=22-124.
DR PDB; 3OR7; X-ray; 2.30 A; C=22-124.
DR PDB; 3PJS; X-ray; 3.80 A; K/L/M/N=22-160.
DR PDB; 3STL; X-ray; 2.40 A; C=22-124.
DR PDB; 3STZ; X-ray; 2.50 A; C=23-124.
DR PDB; 4LBE; X-ray; 2.75 A; C=2-124.
DR PDB; 4LCU; X-ray; 2.75 A; C=2-124.
DR PDB; 4MSW; X-ray; 2.06 A; C=22-124.
DR PDB; 4UUJ; X-ray; 2.40 A; C=22-124.
DR PDB; 5E1A; X-ray; 3.40 A; C=4-124.
DR PDB; 5EBL; X-ray; 2.30 A; C=1-125.
DR PDB; 5EBM; X-ray; 2.50 A; C=1-125.
DR PDB; 5EBW; X-ray; 2.30 A; C=1-123.
DR PDB; 5EC1; X-ray; 2.75 A; C=1-125.
DR PDB; 5EC2; X-ray; 2.30 A; C=1-125.
DR PDB; 5J9P; X-ray; 2.85 A; C=22-117.
DR PDB; 5VK6; X-ray; 2.25 A; C=26-121.
DR PDB; 5VKE; X-ray; 2.37 A; C=26-121.
DR PDB; 5VKH; X-ray; 2.25 A; C=22-124.
DR PDB; 6NFU; X-ray; 2.09 A; C=22-124.
DR PDB; 6NFV; X-ray; 2.13 A; C=22-124.
DR PDB; 6PA0; X-ray; 2.05 A; C=22-124.
DR PDB; 6W0A; X-ray; 3.24 A; C=28-120.
DR PDB; 6W0B; X-ray; 3.60 A; C=28-120.
DR PDB; 6W0C; X-ray; 3.56 A; C=28-120.
DR PDB; 6W0D; X-ray; 3.64 A; C=28-120.
DR PDB; 6W0E; X-ray; 3.51 A; C=28-120.
DR PDB; 6W0F; X-ray; 2.40 A; C=22-124.
DR PDB; 6W0G; X-ray; 2.60 A; C=22-124.
DR PDB; 6W0H; X-ray; 2.60 A; C=22-124.
DR PDB; 6W0I; X-ray; 2.33 A; C=22-124.
DR PDB; 6W0J; X-ray; 2.50 A; C=22-124.
DR PDB; 7M2I; X-ray; 2.69 A; C=26-116.
DR PDB; 7M2J; X-ray; 3.20 A; C=26-116.
DR PDB; 7MDJ; X-ray; 2.75 A; C=1-124.
DR PDB; 7MHX; X-ray; 2.85 A; C=1-124.
DR PDB; 7MJT; X-ray; 3.30 A; C=26-121.
DR PDB; 7MK6; X-ray; 3.10 A; C=26-121.
DR PDB; 7MUB; X-ray; 3.00 A; C=26-121.
DR PDB; 7RP0; X-ray; 2.48 A; C=22-124.
DR PDBsum; 1BL8; -.
DR PDBsum; 1F6G; -.
DR PDBsum; 1J95; -.
DR PDBsum; 1JQ1; -.
DR PDBsum; 1JQ2; -.
DR PDBsum; 1JVM; -.
DR PDBsum; 1K4C; -.
DR PDBsum; 1K4D; -.
DR PDBsum; 1R3I; -.
DR PDBsum; 1R3J; -.
DR PDBsum; 1R3K; -.
DR PDBsum; 1R3L; -.
DR PDBsum; 1ZWI; -.
DR PDBsum; 2A9H; -.
DR PDBsum; 2ATK; -.
DR PDBsum; 2BOB; -.
DR PDBsum; 2BOC; -.
DR PDBsum; 2DWD; -.
DR PDBsum; 2DWE; -.
DR PDBsum; 2H8P; -.
DR PDBsum; 2HG5; -.
DR PDBsum; 2HJF; -.
DR PDBsum; 2HVJ; -.
DR PDBsum; 2HVK; -.
DR PDBsum; 2IH1; -.
DR PDBsum; 2IH3; -.
DR PDBsum; 2ITC; -.
DR PDBsum; 2ITD; -.
DR PDBsum; 2JK5; -.
DR PDBsum; 2NLJ; -.
DR PDBsum; 2P7T; -.
DR PDBsum; 2QTO; -.
DR PDBsum; 2W0F; -.
DR PDBsum; 3EFF; -.
DR PDBsum; 3F5W; -.
DR PDBsum; 3F7V; -.
DR PDBsum; 3F7Y; -.
DR PDBsum; 3FB5; -.
DR PDBsum; 3FB6; -.
DR PDBsum; 3FB7; -.
DR PDBsum; 3FB8; -.
DR PDBsum; 3GB7; -.
DR PDBsum; 3HPL; -.
DR PDBsum; 3IFX; -.
DR PDBsum; 3IGA; -.
DR PDBsum; 3OGC; -.
DR PDBsum; 3OR6; -.
DR PDBsum; 3OR7; -.
DR PDBsum; 3PJS; -.
DR PDBsum; 3STL; -.
DR PDBsum; 3STZ; -.
DR PDBsum; 4LBE; -.
DR PDBsum; 4LCU; -.
DR PDBsum; 4MSW; -.
DR PDBsum; 4UUJ; -.
DR PDBsum; 5E1A; -.
DR PDBsum; 5EBL; -.
DR PDBsum; 5EBM; -.
DR PDBsum; 5EBW; -.
DR PDBsum; 5EC1; -.
DR PDBsum; 5EC2; -.
DR PDBsum; 5J9P; -.
DR PDBsum; 5VK6; -.
DR PDBsum; 5VKE; -.
DR PDBsum; 5VKH; -.
DR PDBsum; 6NFU; -.
DR PDBsum; 6NFV; -.
DR PDBsum; 6PA0; -.
DR PDBsum; 6W0A; -.
DR PDBsum; 6W0B; -.
DR PDBsum; 6W0C; -.
DR PDBsum; 6W0D; -.
DR PDBsum; 6W0E; -.
DR PDBsum; 6W0F; -.
DR PDBsum; 6W0G; -.
DR PDBsum; 6W0H; -.
DR PDBsum; 6W0I; -.
DR PDBsum; 6W0J; -.
DR PDBsum; 7M2I; -.
DR PDBsum; 7M2J; -.
DR PDBsum; 7MDJ; -.
DR PDBsum; 7MHX; -.
DR PDBsum; 7MJT; -.
DR PDBsum; 7MK6; -.
DR PDBsum; 7MUB; -.
DR PDBsum; 7RP0; -.
DR AlphaFoldDB; P0A334; -.
DR BMRB; P0A334; -.
DR PCDDB; P0A334; -.
DR SMR; P0A334; -.
DR DIP; DIP-29626N; -.
DR MINT; P0A334; -.
DR DrugBank; DB07416; (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DR DrugBank; DB01851; Tetrabutylammonium Ion.
DR DrugBank; DB08837; Tetraethylammonium.
DR TCDB; 1.A.1.1.1; the voltage-gated ion channel (vic) superfamily.
DR ABCD; P0A334; 3 sequenced antibodies.
DR EvolutionaryTrace; P0A334; -.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..160
FT /note="pH-gated potassium channel KcsA"
FT /id="PRO_0000054102"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT TRANSMEM 28..50
FT /note="Helical"
FT TOPO_DOM 51..61
FT /note="Extracellular"
FT INTRAMEM 62..72
FT /note="Helical; Pore-forming"
FT INTRAMEM 73..80
FT /note="Pore-forming"
FT TOPO_DOM 81..87
FT /note="Extracellular"
FT TRANSMEM 88..111
FT /note="Helical"
FT TOPO_DOM 112..160
FT /note="Cytoplasmic"
FT MOTIF 75..80
FT /note="Selectivity filter"
FT MUTAGEN 71
FT /note="E->A: Prevents channel inactivation."
FT /evidence="ECO:0000269|PubMed:19959477"
FT HELIX 25..51
FT /evidence="ECO:0007829|PDB:2IH3"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1BL8"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:2IH3"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2IH3"
FT HELIX 86..120
FT /evidence="ECO:0007829|PDB:2IH3"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3OR7"
SQ SEQUENCE 160 AA; 17694 MW; DEBD9E64384BF40C CRC64;
MPPMLSGLLA RLVKLLLGRH GSALHWRAAG AATVLLVIVL LAGSYLAVLA ERGAPGAQLI
TYPRALWWSV ETATTVGYGD LYPVTLWGRL VAVVVMVAGI TSFGLVTAAL ATWFVGREQE
RRGHFVRHSE KAAEEAYTRT TRALHERFDR LERMLDDNRR
