CNGK1_RHIEC
ID CNGK1_RHIEC Reviewed; 355 AA.
AC Q2K5E1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cyclic nucleotide-gated potassium channel RHE_CH03180;
GN OrderedLocusNames=RHE_CH03180;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- FUNCTION: Cyclic nucleotide-regulated potassium channel activated by
CC cAMP. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; CP000133; ABC91945.1; -; Genomic_DNA.
DR RefSeq; WP_011426415.1; NC_007761.1.
DR AlphaFoldDB; Q2K5E1; -.
DR SMR; Q2K5E1; -.
DR STRING; 347834.RHE_CH03180; -.
DR EnsemblBacteria; ABC91945; ABC91945; RHE_CH03180.
DR KEGG; ret:RHE_CH03180; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_011722_1_2_5; -.
DR OMA; MYFIAEG; -.
DR Proteomes; UP000001936; 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: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 3: Inferred from homology;
KW cAMP; cAMP-binding; Cell membrane; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="Cyclic nucleotide-gated potassium channel
FT RHE_CH03180"
FT /id="PRO_0000351502"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 13..30
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 31..38
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..61
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..93
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..111
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 129..149
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 150..160
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 161..179
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..184
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..209
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 210..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 174..179
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT BINDING 297..298
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q98GN8"
FT BINDING 307..308
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q98GN8"
FT BINDING 348
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q98GN8"
SQ SEQUENCE 355 AA; 38298 MW; 1ABFAFC1B84E05D4 CRC64;
MSAVPFSKIS TPLNALFATI GLLVVAALTT QGLTGQERLV FELLLAAIWL AYVLQLSGTL
LSRRRRLSGE MTALVIDLLA VLVPAAAFLF VGSRDRDLYC AIWLLKPLRD STFFRLLAKV
VANESRNLLG VTSVFGIVLF GAALAGYIIE RDVQPDKFGS IPQAMWWAVV TLSTTGYGDE
IPQSLAGRVL AGLVMMSGIG IFALWAGILA TGFYEEVRRQ DFVRNWQLVA AVPLFQKLGS
AALIEIVRAL RPRIVPAGAV ICRKGEVGDQ MFFIVEGRVT VATPDHPVEL GAGNFFGEMA
LISGDPRSAT VSAATEVSLL SLYAVDFQIL SSSSPEIAET IRKTALERRG GPPKE
