KCH_ECOLI
ID KCH_ECOLI Reviewed; 417 AA.
AC P31069; P94716; P94717; P94723; P94729; P97198; P97225;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Voltage-gated potassium channel Kch;
GN Name=kch; OrderedLocusNames=b1250, JW1242;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8170937; DOI=10.1073/pnas.91.9.3510;
RA Milkman R.;
RT "An Escherichia coli homologue of eukaryotic potassium channel proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3510-3514(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12, and Various ECOR strains;
RA Milkman R.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12;
RX PubMed=8824224; DOI=10.1074/jbc.271.42.25912;
RA Johansson M., von Heijne G.;
RT "Membrane topology of Kch, a putative K+ channel from Escherichia coli.";
RL J. Biol. Chem. 271:25912-25915(1996).
RN [7]
RP FUNCTION.
RX PubMed=12912904; DOI=10.1093/emboj/cdg409;
RA Kuo M.M., Saimi Y., Kung C.;
RT "Gain-of-function mutations indicate that Escherichia coli Kch forms a
RT functional K+ conduit in vivo.";
RL EMBO J. 22:4049-4058(2003).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 241-393, AND DIMERIZATION.
RX PubMed=11301020; DOI=10.1016/s0896-6273(01)00236-7;
RA Jiang Y., Pico A., Cadene M., Chait B.T., MacKinnon R.;
RT "Structure of the RCK domain from the E. coli K+ channel and demonstration
RT of its presence in the human BK channel.";
RL Neuron 29:593-601(2001).
CC -!- FUNCTION: K(+)-specific ion channel. May play a role in the defense
CC against osmotic shock. {ECO:0000269|PubMed:12912904,
CC ECO:0000269|PubMed:8170937}.
CC -!- SUBUNIT: Dimer.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8824224};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8824224}.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L12044; AAA66947.1; -; Genomic_DNA.
DR EMBL; U24195; AAB60071.1; -; Genomic_DNA.
DR EMBL; U24196; AAB60079.1; -; Genomic_DNA.
DR EMBL; U24197; AAB60087.1; -; Genomic_DNA.
DR EMBL; U24198; AAB60095.1; -; Genomic_DNA.
DR EMBL; U24199; AAB60103.1; -; Genomic_DNA.
DR EMBL; U24200; AAB60111.1; -; Genomic_DNA.
DR EMBL; U24201; AAB60119.1; -; Genomic_DNA.
DR EMBL; U24202; AAB60127.1; -; Genomic_DNA.
DR EMBL; U24203; AAB60135.1; -; Genomic_DNA.
DR EMBL; U24204; AAB60143.1; -; Genomic_DNA.
DR EMBL; U24205; AAB60151.1; -; Genomic_DNA.
DR EMBL; U24206; AAB60159.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74332.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14782.1; -; Genomic_DNA.
DR PIR; A55252; A55252.
DR PIR; T45507; T45507.
DR RefSeq; NP_415766.1; NC_000913.3.
DR RefSeq; WP_001295624.1; NZ_SSZK01000031.1.
DR PDB; 1ID1; X-ray; 2.40 A; A/B=241-393.
DR PDBsum; 1ID1; -.
DR AlphaFoldDB; P31069; -.
DR SMR; P31069; -.
DR BioGRID; 4261503; 47.
DR DIP; DIP-10055N; -.
DR IntAct; P31069; 1.
DR STRING; 511145.b1250; -.
DR TCDB; 1.A.1.13.1; the voltage-gated ion channel (vic) superfamily.
DR jPOST; P31069; -.
DR PaxDb; P31069; -.
DR PRIDE; P31069; -.
DR EnsemblBacteria; AAC74332; AAC74332; b1250.
DR EnsemblBacteria; BAA14782; BAA14782; BAA14782.
DR GeneID; 945841; -.
DR KEGG; ecj:JW1242; -.
DR KEGG; eco:b1250; -.
DR PATRIC; fig|1411691.4.peg.1033; -.
DR EchoBASE; EB1563; -.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_057267_1_0_6; -.
DR InParanoid; P31069; -.
DR OMA; YGELTEP; -.
DR PhylomeDB; P31069; -.
DR BioCyc; EcoCyc:KCH-MON; -.
DR BioCyc; MetaCyc:KCH-MON; -.
DR EvolutionaryTrace; P31069; -.
DR PRO; PR:P31069; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IMP:EcoCyc.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..417
FT /note="Voltage-gated potassium channel Kch"
FT /id="PRO_0000054096"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..63
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..104
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..110
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..127
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..160
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..199
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:8824224"
FT DOMAIN 245..371
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT MOTIF 185..190
FT /note="Selectivity filter"
FT VARIANT 5
FT /note="A -> T (in strain: ECOR 52 and ECOR 60)"
FT VARIANT 13
FT /note="N -> K (in strain: ECOR 52 and ECOR 60)"
FT VARIANT 223
FT /note="P -> S (in strain: ECOR 4)"
FT VARIANT 405
FT /note="L -> Q (in strain: ECOR 4, ECOR 16, ECOR 28, ECOR
FT 31, ECOR 37, ECOR 46, ECOR 50, ECOR 52, ECOR 60 and ECOR
FT 71)"
FT VARIANT 406
FT /note="E -> K (in strain: ECOR 46)"
FT VARIANT 411
FT /note="S -> N (in strain: ECOR 46)"
FT VARIANT 414
FT /note="S -> L (in strain: ECOR 46)"
FT VARIANT 415
FT /note="A -> V (in strain: ECOR 28)"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:1ID1"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:1ID1"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:1ID1"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:1ID1"
SQ SEQUENCE 417 AA; 46063 MW; B2F803435001FB6E CRC64;
MSHWATFKQT ATNLWVTLRH DILALAVFLN GLLIFKTIYG MSVNLLDIFH IKAFSELDLS
LLANAPLFML GVFLVLNSIG LLFRAKLAWA ISIILLLIAL IYTLHFYPWL KFSIGFCIFT
LVFLLILRKD FSHSSAAAGT IFAFISFTTL LFYSTYGALY LSEGFNPRIE SLMTAFYFSI
ETMSTVGYGD IVPVSESARL FTISVIISGI TVFATSMTSI FGPLIRGGFN KLVKGNNHTM
HRKDHFIVCG HSILAINTIL QLNQRGQNVT VISNLPEDDI KQLEQRLGDN ADVIPGDSND
SSVLKKAGID RCRAILALSD NDADNAFVVL SAKDMSSDVK TVLAVSDSKN LNKIKMVHPD
IILSPQLFGS EILARVLNGE EINNDMLVSM LLNSGHGIFS DNDELETKAD SKESAQK
