MTHK_METTH
ID MTHK_METTH Reviewed; 336 AA.
AC O27564;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcium-gated potassium channel MthK;
GN Name=mthK; OrderedLocusNames=MTH_1520;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), AND MUTAGENESIS OF MET-107 AND
RP ASP-184.
RX PubMed=12037559; DOI=10.1038/417515a;
RA Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R.;
RT "Crystal structure and mechanism of a calcium-gated potassium channel.";
RL Nature 417:515-522(2002).
CC -!- FUNCTION: Calcium-gated potassium channel.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC O27564; O27564: mthK; NbExp=3; IntAct=EBI-1101987, EBI-1101987;
CC O27564-1; O27564-1: mthK; NbExp=11; IntAct=EBI-15621899, EBI-15621899;
CC O27564-2; O27564-2: mthK; NbExp=2; IntAct=EBI-15737903, EBI-15737903;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Calcium-gated potassium channel;
CC IsoId=O27564-1; Sequence=Displayed;
CC Name=Soluble; Synonyms=RCK domain;
CC IsoId=O27564-2; Sequence=VSP_018901;
CC -!- DOMAIN: The channel is composed of 4 repeated units, each containing a
CC transmembrane pore part and a gating ring part. The gating ring is
CC composed of eight identical RCK (Regulators of K conductance) domains,
CC in an alternating arrangement of one domain from each of the four
CC subunits and four from the intracellular solution. Two protein
CC interfaces between dimers of RCK domains from the pore-forming subunit
CC and from the intracellular solution hold the ring together. One is
CC called the fixed interface and the other the flexible interface. The
CC flexible interface forms a cleft where calcium binds. Upon calcium
CC binding the gating ring undergoes a conformational change that enables
CC it to pull open the inner helices of the pore, allowing ion conduction.
CC -!- MISCELLANEOUS: It is not known whether calcium is the physiological
CC ligand.
CC -!- MISCELLANEOUS: Inhibited by charybdotoxin (CTX), a protein from
CC scorpion venom.
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DR EMBL; AE000666; AAB85995.1; -; Genomic_DNA.
DR PIR; H69069; H69069.
DR RefSeq; WP_010877130.1; NC_000916.1.
DR PDB; 1LNQ; X-ray; 3.30 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 2AEF; X-ray; 1.70 A; A/B=107-336.
DR PDB; 2AEJ; X-ray; 2.10 A; A/B=107-336.
DR PDB; 2AEM; X-ray; 2.80 A; A=107-336.
DR PDB; 2FY8; X-ray; 2.79 A; A/B/C/D/E/F/G/H=107-336.
DR PDB; 2OGU; X-ray; 3.23 A; A=107-336.
DR PDB; 3KXD; X-ray; 2.20 A; A/B=116-336.
DR PDB; 3LDC; X-ray; 1.45 A; A=18-99.
DR PDB; 3LDD; X-ray; 1.45 A; A=18-99.
DR PDB; 3LDE; X-ray; 2.21 A; A=18-99.
DR PDB; 3OUS; X-ray; 1.75 A; A=18-99.
DR PDB; 3R65; X-ray; 1.80 A; A=18-99.
DR PDB; 3RBX; X-ray; 2.80 A; A/B/C/D/E/F=107-336.
DR PDB; 3RBZ; X-ray; 3.40 A; A/B/C/D=1-336.
DR PDB; 4EI2; X-ray; 3.11 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=107-336.
DR PDB; 4HYO; X-ray; 1.65 A; A/B/C/D/E/F/G/H=11-101.
DR PDB; 4HZ3; X-ray; 1.70 A; A/B/C/D/E/F/G/H=11-101.
DR PDB; 4L73; X-ray; 2.50 A; A/B=107-336.
DR PDB; 4L74; X-ray; 1.84 A; A/B=107-336.
DR PDB; 4L75; X-ray; 2.39 A; A/B/C/D/E/F=107-336.
DR PDB; 4L76; X-ray; 2.99 A; A/B/C/D/E/F=107-336.
DR PDB; 4QE7; X-ray; 2.40 A; A=19-99.
DR PDB; 4QE9; X-ray; 2.15 A; A=18-100.
DR PDB; 4RO0; X-ray; 3.18 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/a/b/c/d/e/f/g/h/i/j=107-336.
DR PDB; 6OLY; X-ray; 3.11 A; A/B/C/D=1-336.
DR PDB; 6U5N; EM; 3.20 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U5P; EM; 3.30 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U5R; EM; 3.60 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U68; EM; 4.50 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U6D; EM; 3.60 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U6E; EM; 6.30 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U6H; EM; 5.00 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6U9P; X-ray; 1.65 A; A=18-99.
DR PDB; 6U9T; X-ray; 1.55 A; A=18-99.
DR PDB; 6U9Y; X-ray; 1.80 A; A=18-99.
DR PDB; 6U9Z; X-ray; 1.95 A; A=18-99.
DR PDB; 6UWN; EM; 3.50 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6UX4; EM; 3.50 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6UX7; EM; 6.70 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6UXA; EM; 4.50 A; A/B/C/D/E/F/G/H=1-336.
DR PDB; 6UXB; EM; 4.90 A; A/B/C/D/E/F/G/H=1-336.
DR PDBsum; 1LNQ; -.
DR PDBsum; 2AEF; -.
DR PDBsum; 2AEJ; -.
DR PDBsum; 2AEM; -.
DR PDBsum; 2FY8; -.
DR PDBsum; 2OGU; -.
DR PDBsum; 3KXD; -.
DR PDBsum; 3LDC; -.
DR PDBsum; 3LDD; -.
DR PDBsum; 3LDE; -.
DR PDBsum; 3OUS; -.
DR PDBsum; 3R65; -.
DR PDBsum; 3RBX; -.
DR PDBsum; 3RBZ; -.
DR PDBsum; 4EI2; -.
DR PDBsum; 4HYO; -.
DR PDBsum; 4HZ3; -.
DR PDBsum; 4L73; -.
DR PDBsum; 4L74; -.
DR PDBsum; 4L75; -.
DR PDBsum; 4L76; -.
DR PDBsum; 4QE7; -.
DR PDBsum; 4QE9; -.
DR PDBsum; 4RO0; -.
DR PDBsum; 6OLY; -.
DR PDBsum; 6U5N; -.
DR PDBsum; 6U5P; -.
DR PDBsum; 6U5R; -.
DR PDBsum; 6U68; -.
DR PDBsum; 6U6D; -.
DR PDBsum; 6U6E; -.
DR PDBsum; 6U6H; -.
DR PDBsum; 6U9P; -.
DR PDBsum; 6U9T; -.
DR PDBsum; 6U9Y; -.
DR PDBsum; 6U9Z; -.
DR PDBsum; 6UWN; -.
DR PDBsum; 6UX4; -.
DR PDBsum; 6UX7; -.
DR PDBsum; 6UXA; -.
DR PDBsum; 6UXB; -.
DR AlphaFoldDB; O27564; -.
DR SMR; O27564; -.
DR DIP; DIP-37842N; -.
DR TCDB; 1.A.1.13.2; the voltage-gated ion channel (vic) superfamily.
DR EnsemblBacteria; AAB85995; AAB85995; MTH_1520.
DR GeneID; 1471789; -.
DR KEGG; mth:MTH_1520; -.
DR PATRIC; fig|187420.15.peg.1483; -.
DR HOGENOM; CLU_050982_1_0_2; -.
DR OMA; VFEGIWW; -.
DR EvolutionaryTrace; O27564; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.1450; -; 1.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR003148; RCK_N.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF116726; SSF116726; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51202; RCK_C; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Calcium; Cell membrane; Ion channel;
KW Ion transport; Membrane; Metal-binding; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..336
FT /note="Calcium-gated potassium channel MthK"
FT /id="PRO_0000035777"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT TRANSMEM 21..41
FT /note="Helical; Name=Outer helix M1"
FT TOPO_DOM 42..48
FT /note="Extracellular"
FT INTRAMEM 49..58
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000255"
FT INTRAMEM 59..64
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..69
FT /note="Extracellular"
FT TRANSMEM 70..95
FT /note="Helical; Name=Inner helix M2"
FT TOPO_DOM 96..106
FT /note="Cytoplasmic"
FT DOMAIN 117..237
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT DOMAIN 252..336
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT MOTIF 59..64
FT /note="Selectivity filter"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform Soluble)"
FT /evidence="ECO:0000305"
FT /id="VSP_018901"
FT MUTAGEN 107
FT /note="M->I: Elimination of the 26 kDa product and reduced
FT levels of channel expression."
FT /evidence="ECO:0000269|PubMed:12037559"
FT MUTAGEN 184
FT /note="D->N: At high calcium concentration, mean open time
FT is short and mean closed time is long compared with wild-
FT type."
FT /evidence="ECO:0000269|PubMed:12037559"
FT HELIX 20..42
FT /evidence="ECO:0007829|PDB:3LDC"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:3LDC"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3LDD"
FT HELIX 70..98
FT /evidence="ECO:0007829|PDB:3LDC"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6OLY"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:2AEF"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4L75"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:2AEF"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:2FY8"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:2OGU"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2FY8"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2AEF"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:2AEF"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:2AEF"
SQ SEQUENCE 336 AA; 37314 MW; 31FDC5811CB79253 CRC64;
MVLVIEIIRK HLPRVLKVPA TRILLLVLAV IIYGTAGFHF IEGESWTVSL YWTFVTIATV
GYGDYSPSTP LGMYFTVTLI VLGIGTFAVA VERLLEFLIN REQMKLMGLI DVAKSRHVVI
CGWSESTLEC LRELRGSEVF VLAEDENVRK KVLRSGANFV HGDPTRVSDL EKANVRGARA
VIVDLESDSE TIHCILGIRK IDESVRIIAE AERYENIEQL RMAGADQVIS PFVISGRLMS
RSIDDGYEAM FVQDVLAEES TRRMVEVPIP EGSKLEGVSV LDADIHDVTG VIIIGVGRGD
ELIIDPPRDY SFRAGDIILG IGKPEEIERL KNYISA
