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Protein

Cyclic nucleotide-gated potassium channel mll3241

Gene

mll3241

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cyclic nucleotide-regulated potassium channel activated by cAMP.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei348 – 3481cAMP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi297 – 2982cAMP
Nucleotide bindingi307 – 3082cAMP

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Potassium channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-2519-MONOMER.

Protein family/group databases

TCDBi1.A.1.25.1. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic nucleotide-gated potassium channel mll3241
Alternative name(s):
MlotiK1 channel
Gene namesi
Ordered Locus Names:mll3241
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
Proteomesi
  • UP000000552 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicAdd
BLAST
Transmembranei13 – 3018Helical; Name=Segment S1Add
BLAST
Topological domaini31 – 388Periplasmic
Transmembranei39 – 6123Helical; Name=Segment S2Add
BLAST
Topological domaini62 – 7413CytoplasmicAdd
BLAST
Transmembranei75 – 9420Helical; Name=Segment S3Add
BLAST
Transmembranei95 – 11218Helical; Name=Segment S4Add
BLAST
Topological domaini113 – 12917CytoplasmicAdd
BLAST
Transmembranei130 – 15021Helical; Name=Segment S5Add
BLAST
Topological domaini151 – 16111PeriplasmicAdd
BLAST
Intramembranei162 – 18019Pore-formingAdd
BLAST
Topological domaini181 – 1855Periplasmic
Transmembranei186 – 21025Helical; Name=Segment S6Add
BLAST
Topological domaini211 – 355145CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi203 – 2031F → A: Increased channel conductance. 1 Publication
Mutagenesisi215 – 2151Y → A: Increased channel conductance. 1 Publication
Mutagenesisi227 – 2271W → A: Loss of channel activity. 1 Publication
Mutagenesisi348 – 3481R → A: Loss of cAMP binding. Loss of channel activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Cyclic nucleotide-gated potassium channel mll3241PRO_0000351501Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-29507N.
STRINGi266835.mll3241.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Helixi13 – 2816Combined sources
Beta strandi30 – 323Combined sources
Helixi35 – 6127Combined sources
Helixi72 – 9019Combined sources
Helixi95 – 10511Combined sources
Helixi107 – 1104Combined sources
Helixi115 – 12410Combined sources
Helixi126 – 15126Combined sources
Turni152 – 1543Combined sources
Helixi156 – 1594Combined sources
Helixi162 – 17312Combined sources
Beta strandi179 – 1813Combined sources
Helixi216 – 2238Combined sources
Helixi226 – 2305Combined sources
Helixi234 – 2385Combined sources
Helixi241 – 25010Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi280 – 2867Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi295 – 2973Combined sources
Helixi298 – 3036Combined sources
Beta strandi308 – 32316Combined sources
Helixi324 – 33310Combined sources
Helixi335 – 35218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U12X-ray2.70A/B218-355[»]
1VP6X-ray1.70A/C218-355[»]
2K0GNMR-A216-355[»]
2KXLNMR-A216-355[»]
2ZD9X-ray4.00A/B/C/D1-355[»]
3BEHX-ray3.10A/B/C/D1-355[»]
3CL1X-ray2.40A/B216-355[»]
3CLPX-ray2.00A/C216-355[»]
3CO2X-ray2.90A/B/C/D216-355[»]
4CHVelectron microscopy7.00A/B/C/D1-355[»]
4CHWelectron microscopy7.00A/B/C/D1-355[»]
4MUVX-ray1.25A/B216-355[»]
ProteinModelPortaliQ98GN8.
SMRiQ98GN8. Positions 5-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ98GN8.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi175 – 1806Selectivity filterCurated

Sequence similaritiesi

Belongs to the potassium channel family.Curated
Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EYW. Bacteria.
COG0664. LUCA.
COG1226. LUCA.
HOGENOMiHOG000271293.
KOiK10716.
OMAiMMSGIGI.
OrthoDBiEOG6DJZ5S.

Family and domain databases

Gene3Di1.20.120.540. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR013099. K_chnl_dom.
IPR027378. Nucleotide_channel_N.
IPR014710. RmlC-like_jellyroll.
IPR028325. VG_K_chnl.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF07885. Ion_trans_2. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q98GN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVLPFLRIY APLNAVLAAP GLLAVAALTI PDMSGRSRLA LAALLAVIWG
60 70 80 90 100
AYLLQLAATL LKRRAGVVRD RTPKIAIDVL AVLVPLAAFL LDGSPDWSLY
110 120 130 140 150
CAVWLLKPLR DSTFFPVLGR VLANEARNLI GVTTLFGVVL FAVALAAYVI
160 170 180 190 200
ERDIQPEKFG SIPQAMWWAV VTLSTTGYGD TIPQSFAGRV LAGAVMMSGI
210 220 230 240 250
GIFGLWAGIL ATGFYQEVRR GDFVRNWQLV AAVPLFQKLG PAVLVEIVRA
260 270 280 290 300
LRARTVPAGA VICRIGEPGD RMFFVVEGSV SVATPNPVEL GPGAFFGEMA
310 320 330 340 350
LISGEPRSAT VSAATTVSLL SLHSADFQML CSSSPEIAEI FRKTALERRG

AAASA
Length:355
Mass (Da):37,735
Last modified:October 1, 2001 - v1
Checksum:i35EE06373D563933
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50178.1.
RefSeqiWP_010911524.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB50178; BAB50178; BAB50178.
GeneIDi1227053.
KEGGimlo:mll3241.
PATRICi22479361. VBIMesLot2464_2584.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50178.1.
RefSeqiWP_010911524.1. NC_002678.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U12X-ray2.70A/B218-355[»]
1VP6X-ray1.70A/C218-355[»]
2K0GNMR-A216-355[»]
2KXLNMR-A216-355[»]
2ZD9X-ray4.00A/B/C/D1-355[»]
3BEHX-ray3.10A/B/C/D1-355[»]
3CL1X-ray2.40A/B216-355[»]
3CLPX-ray2.00A/C216-355[»]
3CO2X-ray2.90A/B/C/D216-355[»]
4CHVelectron microscopy7.00A/B/C/D1-355[»]
4CHWelectron microscopy7.00A/B/C/D1-355[»]
4MUVX-ray1.25A/B216-355[»]
ProteinModelPortaliQ98GN8.
SMRiQ98GN8. Positions 5-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29507N.
STRINGi266835.mll3241.

Protein family/group databases

TCDBi1.A.1.25.1. the voltage-gated ion channel (vic) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB50178; BAB50178; BAB50178.
GeneIDi1227053.
KEGGimlo:mll3241.
PATRICi22479361. VBIMesLot2464_2584.

Phylogenomic databases

eggNOGiENOG4105EYW. Bacteria.
COG0664. LUCA.
COG1226. LUCA.
HOGENOMiHOG000271293.
KOiK10716.
OMAiMMSGIGI.
OrthoDBiEOG6DJZ5S.

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-2519-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ98GN8.

Family and domain databases

Gene3Di1.20.120.540. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR013099. K_chnl_dom.
IPR027378. Nucleotide_channel_N.
IPR014710. RmlC-like_jellyroll.
IPR028325. VG_K_chnl.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF07885. Ion_trans_2. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MAFF303099.
  2. "Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel."
    Clayton G.M., Silverman W.R., Heginbotham L., Morais-Cabral J.H.
    Cell 119:615-627(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 218-355 IN COMPLEXES WITH CAMP, FUNCTION, SUBUNIT, MUTAGENESIS OF TRP-227 AND ARG-348.
  3. "Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel."
    Clayton G.M., Altieri S., Heginbotham L., Unger V.M., Morais-Cabral J.H.
    Proc. Natl. Acad. Sci. U.S.A. 105:1511-1515(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), MEMBRANE TOPOLOGY, MUTAGENESIS OF PHE-203 AND TYR-215.

Entry informationi

Entry nameiCNGK1_RHILO
AccessioniPrimary (citable) accession number: Q98GN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 1, 2001
Last modified: January 20, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.