ID KCSA_STRCO Reviewed; 160 AA.
AC P0A333; Q54397;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=pH-gated potassium channel KcsA;
GN Name=kcsA; Synonyms=skc1; OrderedLocusNames=SCO7660; ORFNames=SC10F4.33;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Acts as a pH-gated potassium ion channel; changing the
CC cytosolic pH from 7 to 4 opens the channel. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The cytoplasmic C-terminus is involved in the gating mechanism.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The amino acids 62-79 are situated in the membrane and
CC are important for channel structure and properties. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; AL939132; CAC16993.1; -; Genomic_DNA.
DR RefSeq; NP_631700.1; NC_003888.3.
DR RefSeq; WP_003971485.1; NZ_VNID01000005.1.
DR PDB; 1S5H; X-ray; 2.20 A; C=3-124.
DR PDB; 2HFE; X-ray; 2.25 A; C=22-78, D=80-122.
DR PDB; 6BY2; X-ray; 2.35 A; C=22-116.
DR PDB; 6BY3; X-ray; 2.37 A; C=26-116.
DR PDB; 7SQW; X-ray; 3.21 A; C=22-124.
DR PDBsum; 1S5H; -.
DR PDBsum; 2HFE; -.
DR PDBsum; 6BY2; -.
DR PDBsum; 6BY3; -.
DR PDBsum; 7SQW; -.
DR AlphaFoldDB; P0A333; -.
DR BMRB; P0A333; -.
DR SMR; P0A333; -.
DR STRING; 100226.gene:17765320; -.
DR DrugBank; DB07416; (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DR PaxDb; 100226-SCO7660; -.
DR ABCD; P0A333; 1 sequenced antibody.
DR PATRIC; fig|100226.15.peg.7779; -.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_1618042_0_0_11; -.
DR InParanoid; P0A333; -.
DR OrthoDB; 9799090at2; -.
DR PhylomeDB; P0A333; -.
DR EvolutionaryTrace; P0A333; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.5.440; ATP synthase delta/epsilon subunit, C-terminal domain; 1.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11537:SF254; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN SHAKER; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..160
FT /note="pH-gated potassium channel KcsA"
FT /id="PRO_0000054101"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 51..61
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 62..72
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000255"
FT INTRAMEM 73..80
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..87
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 88..111
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 75..80
FT /note="Selectivity filter"
FT HELIX 24..51
FT /evidence="ECO:0007829|PDB:1S5H"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:1S5H"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1S5H"
FT HELIX 86..121
FT /evidence="ECO:0007829|PDB:1S5H"
SQ SEQUENCE 160 AA; 17694 MW; DEBD9E64384BF40C CRC64;
MPPMLSGLLA RLVKLLLGRH GSALHWRAAG AATVLLVIVL LAGSYLAVLA ERGAPGAQLI
TYPRALWWSV ETATTVGYGD LYPVTLWGRL VAVVVMVAGI TSFGLVTAAL ATWFVGREQE
RRGHFVRHSE KAAEEAYTRT TRALHERFDR LERMLDDNRR
//
