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Protein

Calcium-gated potassium channel MthK

Gene

mthK

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-gated potassium channel.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi184Calcium1
Metal bindingi210Calcium1
Metal bindingi212Calcium1

GO - Molecular functioni

  • cation transmembrane transporter activity Source: InterPro
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calcium, Metal-binding, Potassium

Protein family/group databases

TCDBi1.A.1.13.2. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-gated potassium channel MthK
Gene namesi
Name:mthK
Ordered Locus Names:MTH_1520
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20CytoplasmicAdd BLAST20
Transmembranei21 – 41Helical; Name=Outer helix M1Add BLAST21
Topological domaini42 – 48Extracellular7
Intramembranei49 – 58Helical; Pore-formingSequence analysis10
Intramembranei59 – 64Pore-formingSequence analysis6
Topological domaini65 – 69Extracellular5
Transmembranei70 – 95Helical; Name=Inner helix M2Add BLAST26
Topological domaini96 – 106CytoplasmicAdd BLAST11

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107M → I: Elimination of the 26 kDa product and reduced levels of channel expression. 1 Publication1
Mutagenesisi184D → N: At high calcium concentration, mean open time is short and mean closed time is long compared with wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000357771 – 336Calcium-gated potassium channel MthKAdd BLAST336

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1101987,EBI-1101987

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-37842N.
STRINGi187420.MTH1520.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 42Combined sources23
Helixi46 – 57Combined sources12
Beta strandi63 – 65Combined sources3
Helixi70 – 98Combined sources29
Beta strandi117 – 122Combined sources6
Helixi125 – 133Combined sources9
Turni134 – 136Combined sources3
Beta strandi137 – 144Combined sources8
Helixi146 – 148Combined sources3
Helixi149 – 154Combined sources6
Beta strandi158 – 162Combined sources5
Helixi167 – 172Combined sources6
Beta strandi179 – 183Combined sources5
Helixi188 – 201Combined sources14
Beta strandi203 – 210Combined sources8
Helixi214 – 216Combined sources3
Helixi217 – 223Combined sources7
Beta strandi226 – 229Combined sources4
Helixi231 – 241Combined sources11
Turni242 – 245Combined sources4
Helixi247 – 256Combined sources10
Beta strandi257 – 261Combined sources5
Beta strandi263 – 268Combined sources6
Beta strandi271 – 273Combined sources3
Turni274 – 277Combined sources4
Helixi280 – 283Combined sources4
Helixi285 – 289Combined sources5
Beta strandi292 – 298Combined sources7
Beta strandi301 – 305Combined sources5
Beta strandi317 – 322Combined sources6
Helixi324 – 334Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LNQX-ray3.30A/B/C/D/E/F/G/H1-336[»]
2AEFX-ray1.70A/B107-336[»]
2AEJX-ray2.10A/B107-336[»]
2AEMX-ray2.80A107-336[»]
2FY8X-ray2.79A/B/C/D/E/F/G/H107-336[»]
2OGUX-ray3.23A107-336[»]
3KXDX-ray2.20A/B116-336[»]
3LDCX-ray1.45A18-99[»]
3LDDX-ray1.45A18-99[»]
3LDEX-ray2.21A18-99[»]
3OUSX-ray1.75A18-99[»]
3R65X-ray1.80A18-99[»]
3RBXX-ray2.80A/B/C/D/E/F107-336[»]
3RBZX-ray3.40A/B/C/D1-336[»]
4EI2X-ray3.11A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P107-336[»]
4HYOX-ray1.65A/B/C/D/E/F/G/H11-101[»]
4HZ3X-ray1.70A/B/C/D/E/F/G/H11-101[»]
4L73X-ray2.50A/B107-336[»]
4L74X-ray1.84A/B107-336[»]
4L75X-ray2.39A/B/C/D/E/F107-336[»]
4L76X-ray2.99A/B/C/D/E/F107-336[»]
4QE7X-ray2.40A19-99[»]
4QE9X-ray2.15A18-100[»]
4RO0X-ray3.18A/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/j107-336[»]
ProteinModelPortaliO27564.
SMRiO27564.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO27564.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini117 – 237RCK N-terminalPROSITE-ProRule annotationAdd BLAST121
Domaini252 – 336RCK C-terminalPROSITE-ProRule annotationAdd BLAST85

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi59 – 64Selectivity filter6

Domaini

The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.

Sequence similaritiesi

Contains 1 RCK C-terminal domain.PROSITE-ProRule annotation
Contains 1 RCK N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG01958. Archaea.
COG1226. LUCA.
KOiK10716.
OMAiFVVCYHN.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF07885. Ion_trans_2. 1 hit.
PF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: O27564-1) [UniParc]FASTAAdd to basket
Also known as: Calcium-gated potassium channel

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVLVIEIIRK HLPRVLKVPA TRILLLVLAV IIYGTAGFHF IEGESWTVSL
60 70 80 90 100
YWTFVTIATV GYGDYSPSTP LGMYFTVTLI VLGIGTFAVA VERLLEFLIN
110 120 130 140 150
REQMKLMGLI DVAKSRHVVI CGWSESTLEC LRELRGSEVF VLAEDENVRK
160 170 180 190 200
KVLRSGANFV HGDPTRVSDL EKANVRGARA VIVDLESDSE TIHCILGIRK
210 220 230 240 250
IDESVRIIAE AERYENIEQL RMAGADQVIS PFVISGRLMS RSIDDGYEAM
260 270 280 290 300
FVQDVLAEES TRRMVEVPIP EGSKLEGVSV LDADIHDVTG VIIIGVGRGD
310 320 330
ELIIDPPRDY SFRAGDIILG IGKPEEIERL KNYISA
Length:336
Mass (Da):37,314
Last modified:January 1, 1998 - v1
Checksum:i31FDC5811CB79253
GO
Isoform Soluble (identifier: O27564-2) [UniParc]FASTAAdd to basket
Also known as: RCK domain

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Note: No experimental confirmation available.
Show »
Length:230
Mass (Da):25,416
Checksum:i90462DA6E2BC1649
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189011 – 106Missing in isoform Soluble. CuratedAdd BLAST106

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85995.1.
PIRiH69069.
RefSeqiWP_010877130.1. NC_000916.1. [O27564-1]

Genome annotation databases

EnsemblBacteriaiAAB85995; AAB85995; MTH_1520.
GeneIDi1471789.
KEGGimth:MTH_1520.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85995.1.
PIRiH69069.
RefSeqiWP_010877130.1. NC_000916.1. [O27564-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LNQX-ray3.30A/B/C/D/E/F/G/H1-336[»]
2AEFX-ray1.70A/B107-336[»]
2AEJX-ray2.10A/B107-336[»]
2AEMX-ray2.80A107-336[»]
2FY8X-ray2.79A/B/C/D/E/F/G/H107-336[»]
2OGUX-ray3.23A107-336[»]
3KXDX-ray2.20A/B116-336[»]
3LDCX-ray1.45A18-99[»]
3LDDX-ray1.45A18-99[»]
3LDEX-ray2.21A18-99[»]
3OUSX-ray1.75A18-99[»]
3R65X-ray1.80A18-99[»]
3RBXX-ray2.80A/B/C/D/E/F107-336[»]
3RBZX-ray3.40A/B/C/D1-336[»]
4EI2X-ray3.11A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P107-336[»]
4HYOX-ray1.65A/B/C/D/E/F/G/H11-101[»]
4HZ3X-ray1.70A/B/C/D/E/F/G/H11-101[»]
4L73X-ray2.50A/B107-336[»]
4L74X-ray1.84A/B107-336[»]
4L75X-ray2.39A/B/C/D/E/F107-336[»]
4L76X-ray2.99A/B/C/D/E/F107-336[»]
4QE7X-ray2.40A19-99[»]
4QE9X-ray2.15A18-100[»]
4RO0X-ray3.18A/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/j107-336[»]
ProteinModelPortaliO27564.
SMRiO27564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37842N.
STRINGi187420.MTH1520.

Protein family/group databases

TCDBi1.A.1.13.2. the voltage-gated ion channel (vic) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85995; AAB85995; MTH_1520.
GeneIDi1471789.
KEGGimth:MTH_1520.

Phylogenomic databases

eggNOGiarCOG01958. Archaea.
COG1226. LUCA.
KOiK10716.
OMAiFVVCYHN.

Miscellaneous databases

EvolutionaryTraceiO27564.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF07885. Ion_trans_2. 1 hit.
PF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTHK_METTH
AccessioniPrimary (citable) accession number: O27564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not known whether calcium is the physiological ligand.
Inhibited by charybdotoxin (CTX), a protein from scorpion venom.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.