CNGK1_RHILO
ID CNGK1_RHILO Reviewed; 355 AA.
AC Q98GN8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cyclic nucleotide-gated potassium channel mll3241;
DE AltName: Full=MlotiK1 channel;
GN OrderedLocusNames=mll3241;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
RN [2] {ECO:0007744|PDB:1U12, ECO:0007744|PDB:1VP6}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 218-355 IN COMPLEXES WITH CAMP,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF TRP-227 AND ARG-348.
RX PubMed=15550244; DOI=10.1016/j.cell.2004.10.030;
RA Clayton G.M., Silverman W.R., Heginbotham L., Morais-Cabral J.H.;
RT "Structural basis of ligand activation in a cyclic nucleotide regulated
RT potassium channel.";
RL Cell 119:615-627(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), MEMBRANE TOPOLOGY, AND MUTAGENESIS
RP OF PHE-203 AND TYR-215.
RX PubMed=18216238; DOI=10.1073/pnas.0711533105;
RA Clayton G.M., Altieri S., Heginbotham L., Unger V.M., Morais-Cabral J.H.;
RT "Structure of the transmembrane regions of a bacterial cyclic nucleotide-
RT regulated channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1511-1515(2008).
CC -!- FUNCTION: Cyclic nucleotide-regulated potassium channel activated by
CC cAMP. {ECO:0000269|PubMed:15550244}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15550244}.
CC -!- INTERACTION:
CC Q98GN8; Q98GN8: mll3241; NbExp=2; IntAct=EBI-15658025, EBI-15658025;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; BA000012; BAB50178.1; -; Genomic_DNA.
DR RefSeq; WP_010911524.1; NC_002678.2.
DR PDB; 1U12; X-ray; 2.70 A; A/B=218-355.
DR PDB; 1VP6; X-ray; 1.70 A; A/C=218-355.
DR PDB; 2K0G; NMR; -; A=216-355.
DR PDB; 2KXL; NMR; -; A=216-355.
DR PDB; 2ZD9; X-ray; 4.00 A; A/B/C/D=1-355.
DR PDB; 3BEH; X-ray; 3.10 A; A/B/C/D=1-355.
DR PDB; 3CL1; X-ray; 2.40 A; A/B=216-355.
DR PDB; 3CLP; X-ray; 2.00 A; A/C=216-355.
DR PDB; 3CO2; X-ray; 2.90 A; A/B/C/D=216-355.
DR PDB; 4CHV; EM; 7.00 A; A/B/C/D=1-355.
DR PDB; 4CHW; EM; 7.00 A; A/B/C/D=1-355.
DR PDB; 4MUV; X-ray; 1.25 A; A/B=216-355.
DR PDB; 6EO1; EM; 4.50 A; A/B/C/D=1-355.
DR PDB; 6I9D; EM; 4.00 A; A/B/C/D=1-355.
DR PDB; 6IAX; EM; 5.20 A; A/B/C/D=1-355.
DR PDB; 6M63; X-ray; 2.25 A; A/B=213-284.
DR PDB; 6QCY; EM; 4.70 A; A/B/C/D=1-355.
DR PDB; 6QCZ; EM; 4.40 A; A/B/C/D=1-355.
DR PDB; 6QD0; EM; 4.50 A; A/B/C/D=1-355.
DR PDB; 6QD1; EM; 5.40 A; A/B/C/D=1-355.
DR PDB; 6QD2; EM; 4.80 A; A/B/C/D=1-355.
DR PDB; 6QD3; EM; 5.00 A; A/B/C/D=1-355.
DR PDB; 6QD4; EM; 5.60 A; A/B/C/D=1-355.
DR PDBsum; 1U12; -.
DR PDBsum; 1VP6; -.
DR PDBsum; 2K0G; -.
DR PDBsum; 2KXL; -.
DR PDBsum; 2ZD9; -.
DR PDBsum; 3BEH; -.
DR PDBsum; 3CL1; -.
DR PDBsum; 3CLP; -.
DR PDBsum; 3CO2; -.
DR PDBsum; 4CHV; -.
DR PDBsum; 4CHW; -.
DR PDBsum; 4MUV; -.
DR PDBsum; 6EO1; -.
DR PDBsum; 6I9D; -.
DR PDBsum; 6IAX; -.
DR PDBsum; 6M63; -.
DR PDBsum; 6QCY; -.
DR PDBsum; 6QCZ; -.
DR PDBsum; 6QD0; -.
DR PDBsum; 6QD1; -.
DR PDBsum; 6QD2; -.
DR PDBsum; 6QD3; -.
DR PDBsum; 6QD4; -.
DR AlphaFoldDB; Q98GN8; -.
DR BMRB; Q98GN8; -.
DR SMR; Q98GN8; -.
DR DIP; DIP-29507N; -.
DR STRING; 266835.14023572; -.
DR DrugBank; DB02527; Cyclic adenosine monophosphate.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.A.1.25.1; the voltage-gated ion channel (vic) superfamily.
DR EnsemblBacteria; BAB50178; BAB50178; BAB50178.
DR KEGG; mlo:mll3241; -.
DR PATRIC; fig|266835.9.peg.2584; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_011722_1_2_5; -.
DR OMA; MYFIAEG; -.
DR OrthoDB; 1991946at2; -.
DR EvolutionaryTrace; Q98GN8; -.
DR Proteomes; UP000000552; 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:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.20.120.540; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR027378; Nucleotide_channel_N.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; cAMP; cAMP-binding; Cell membrane; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Potassium; Potassium channel; Potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="Cyclic nucleotide-gated potassium channel mll3241"
FT /id="PRO_0000351501"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT TRANSMEM 13..30
FT /note="Helical; Name=Segment S1"
FT TOPO_DOM 31..38
FT /note="Periplasmic"
FT TRANSMEM 39..61
FT /note="Helical; Name=Segment S2"
FT TOPO_DOM 62..74
FT /note="Cytoplasmic"
FT TRANSMEM 75..94
FT /note="Helical; Name=Segment S3"
FT TRANSMEM 95..112
FT /note="Helical; Name=Segment S4"
FT TOPO_DOM 113..129
FT /note="Cytoplasmic"
FT TRANSMEM 130..150
FT /note="Helical; Name=Segment S5"
FT TOPO_DOM 151..161
FT /note="Periplasmic"
FT INTRAMEM 162..180
FT /note="Pore-forming"
FT TOPO_DOM 181..185
FT /note="Periplasmic"
FT TRANSMEM 186..210
FT /note="Helical; Name=Segment S6"
FT TOPO_DOM 211..355
FT /note="Cytoplasmic"
FT MOTIF 175..180
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT BINDING 297..298
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0007744|PDB:1VP6"
FT BINDING 307..308
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0007744|PDB:1VP6"
FT BINDING 348
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0007744|PDB:1VP6"
FT MUTAGEN 203
FT /note="F->A: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:18216238"
FT MUTAGEN 215
FT /note="Y->A: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:18216238"
FT MUTAGEN 227
FT /note="W->A: Loss of channel activity."
FT /evidence="ECO:0000269|PubMed:15550244"
FT MUTAGEN 348
FT /note="R->A: Loss of cAMP binding. Loss of channel
FT activity."
FT /evidence="ECO:0000269|PubMed:15550244"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3BEH"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 35..61
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 126..151
FT /evidence="ECO:0007829|PDB:3BEH"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:3BEH"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3BEH"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:4MUV"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:4MUV"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4MUV"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3CLP"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4MUV"
FT STRAND 308..323
FT /evidence="ECO:0007829|PDB:4MUV"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:4MUV"
FT HELIX 335..352
FT /evidence="ECO:0007829|PDB:4MUV"
SQ SEQUENCE 355 AA; 37735 MW; 35EE06373D563933 CRC64;
MSVLPFLRIY APLNAVLAAP GLLAVAALTI PDMSGRSRLA LAALLAVIWG AYLLQLAATL
LKRRAGVVRD RTPKIAIDVL AVLVPLAAFL LDGSPDWSLY CAVWLLKPLR DSTFFPVLGR
VLANEARNLI GVTTLFGVVL FAVALAAYVI ERDIQPEKFG SIPQAMWWAV VTLSTTGYGD
TIPQSFAGRV LAGAVMMSGI GIFGLWAGIL ATGFYQEVRR GDFVRNWQLV AAVPLFQKLG
PAVLVEIVRA LRARTVPAGA VICRIGEPGD RMFFVVEGSV SVATPNPVEL GPGAFFGEMA
LISGEPRSAT VSAATTVSLL SLHSADFQML CSSSPEIAEI FRKTALERRG AAASA
