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KCSA_STRCO
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   25-MAY-2022, entry version 102.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   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   PDBsum; 1S5H; -.
DR   PDBsum; 2HFE; -.
DR   PDBsum; 6BY2; -.
DR   PDBsum; 6BY3; -.
DR   AlphaFoldDB; P0A333; -.
DR   BMRB; P0A333; -.
DR   SMR; P0A333; -.
DR   STRING; 100226.SCO7660; -.
DR   DrugBank; DB07416; (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DR   ABCD; P0A333; 1 sequenced antibody.
DR   GeneID; 1103098; -.
DR   KEGG; sco:SCO7660; -.
DR   PATRIC; fig|100226.15.peg.7779; -.
DR   eggNOG; COG1226; Bacteria.
DR   HOGENOM; CLU_1618042_0_0_11; -.
DR   InParanoid; P0A333; -.
DR   OMA; WFVGREQ; -.
DR   PhylomeDB; P0A333; -.
DR   EvolutionaryTrace; P0A333; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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; 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
 
 
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