MSCK_ECOLI
ID MSCK_ECOLI Reviewed; 1120 AA.
AC P77338; Q2MBW2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mechanosensitive channel MscK;
DE AltName: Full=Potassium efflux system KefA;
DE Flags: Precursor;
GN Name=mscK; Synonyms=aefA, kefA; OrderedLocusNames=b0465, JW0454;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Jones M.A., McLaggen D., Epstein W., Booth I.R.;
RT "Characterisation of the aefA locus of E.coli.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RC STRAIN=K12 / MJF379;
RX PubMed=10202137; DOI=10.1093/emboj/18.7.1730;
RA Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A., Booth I.R.;
RT "Protection of Escherichia coli cells against extreme turgor by activation
RT of MscS and MscL mechanosensitive channels: identification of genes
RT required for MscS activity.";
RL EMBO J. 18:1730-1737(1999).
RN [6]
RP FUNCTION, AND GENE NAME.
RX PubMed=12374733; DOI=10.1093/emboj/cdf537;
RA Li Y., Moe P.C., Chandrasekaran S., Booth I.R., Blount P.;
RT "Ionic regulation of MscK, a mechanosensitive channel from Escherichia
RT coli.";
RL EMBO J. 21:5323-5330(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF GLY-922.
RC STRAIN=K12;
RX PubMed=11985727; DOI=10.1046/j.1365-2958.2002.02764.x;
RA McLaggan D., Jones M.A., Gouesbet G., Levina N., Lindey S., Epstein W.,
RA Booth I.R.;
RT "Analysis of the kefA2 mutation suggests that KefA is a cation-specific
RT channel involved in osmotic adaptation in Escherichia coli.";
RL Mol. Microbiol. 43:521-536(2002).
RN [8]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Mechanosensitive channel that opens in response to membrane
CC tension and specific ionic conditions. Requires high concentrations of
CC external K(+), NH(4)(+), Rb(+) or Cs(+) to gate. May participate in the
CC regulation of osmotic pressure changes within the cell, although it
CC does not appear to have a major role in osmolarity regulation. Forms an
CC ion channel of 1.0 nanosiemens conductance. The channel can remain
CC active for between 30 seconds and over 3 minutes; it does not
CC desensitize upon extended pressure. Its activity is masked in wild-type
CC cells by the MscS channel. {ECO:0000269|PubMed:10202137,
CC ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:12374733}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11985727,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; Y07802; CAA69140.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40219.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73567.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76244.1; -; Genomic_DNA.
DR PIR; H64776; H64776.
DR RefSeq; NP_414998.1; NC_000913.3.
DR RefSeq; WP_000177732.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P77338; -.
DR SMR; P77338; -.
DR BioGRID; 4259842; 274.
DR DIP; DIP-10070N; -.
DR IntAct; P77338; 3.
DR STRING; 511145.b0465; -.
DR TCDB; 1.A.23.1.1; the small conductance mechanosensitive ion channel (mscs) family.
DR jPOST; P77338; -.
DR PaxDb; P77338; -.
DR PRIDE; P77338; -.
DR EnsemblBacteria; AAC73567; AAC73567; b0465.
DR EnsemblBacteria; BAE76244; BAE76244; BAE76244.
DR GeneID; 945132; -.
DR KEGG; ecj:JW0454; -.
DR KEGG; eco:b0465; -.
DR PATRIC; fig|1411691.4.peg.1811; -.
DR EchoBASE; EB3991; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG3264; Bacteria.
DR HOGENOM; CLU_007829_3_0_6; -.
DR InParanoid; P77338; -.
DR OMA; YWVWSDL; -.
DR PhylomeDB; P77338; -.
DR BioCyc; EcoCyc:G6255-MON; -.
DR PRO; PR:P77338; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:EcoCyc.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0035864; P:response to potassium ion; IDA:EcoCyc.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR011066; MscS_channel_C.
DR InterPro; IPR006686; MscS_channel_CS.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR025692; MscS_IM_dom1.
DR InterPro; IPR024393; MscS_porin.
DR Pfam; PF00924; MS_channel; 1.
DR Pfam; PF12795; MscS_porin; 1.
DR Pfam; PF12794; MscS_TM; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR SUPFAM; SSF82689; SSF82689; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
DR PROSITE; PS01246; UPF0003; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Coiled coil; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1120
FT /note="Mechanosensitive channel MscK"
FT /id="PRO_0000043366"
FT TOPO_DOM 34..499
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..657
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..728
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..839
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 908..921
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..1120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 43..98
FT /evidence="ECO:0000255"
FT COILED 126..266
FT /evidence="ECO:0000255"
FT COILED 360..422
FT /evidence="ECO:0000255"
FT COILED 1057..1081
FT /evidence="ECO:0000255"
FT MUTAGEN 922
FT /note="G->S: Prevents growth in medium containing high
FT levels of potassium in the presence of betaine."
FT /evidence="ECO:0000269|PubMed:11985727"
SQ SEQUENCE 1120 AA; 127215 MW; 809895660D2BD444 CRC64;
MTMFQYYKRS RHFVFSAFIA FVFVLLCQNT AFARASSNGD LPTKADLQAQ LDSLNKQKDL
SAQDKLVQQD LTDTLATLDK IDRIKEETVQ LRQKVAEAPE KMRQATAALT ALSDVDNDEE
TRKILSTLSL RQLETRVAQA LDDLQNAQND LASYNSQLVS LQTQPERVQN AMYNASQQLQ
QIRSRLDGTD VGETALRPSQ KVLMQAQQAL LNAEIDQQRK SLEGNTVLQD TLQKQRDYVT
ANSARLEHQL QLLQEAVNSK RLTLTEKTAQ EAVSPDEAAR IQANPLVKQE LEINQQLSQR
LITATENGNQ LMQQNIKVKN WLERALQSER NIKEQIAVLK GSLLLSRILY QQQQTLPSAD
ELENMTNRIA DLRLEQFEVN QQRDALFQSD AFVNKLEEGH TNEVNSEVHD ALLQVVDMRR
ELLDQLNKQL GNQLMMAINL QINQQQLMSV SKNLKSILTQ QIFWVNSNRP MDWDWIKAFP
QSLKDEFKSM KITVNWQKAW PAVFIAFLAG LPLLLIAGLI HWRLGWLKAY QQKLASAVGS
LRNDSQLNTP KAILIDLIRA LPVCLIILAV GLILLTMQLN ISELLWSFSK KLAIFWLVFG
LCWKVLEKNG VAVRHFGMPE QQTSHWRRQI VRISLALLPI HFWSVVAELS PLHLMDDVLG
QAMIFFNLLL IAFLVWPMCR ESWRDKESHT MRLVTITVLS IIPIALMVLT ATGYFYTTLR
LAGRWIETVY LVIIWNLLYQ TVLRGLSVAA RRIAWRRALA RRQNLVKEGA EGAEPPEEPT
IALEQVNQQT LRITMLLMFA LFGVMFWAIW SDLITVFSYL DSITLWHYNG TEAGAAVVKN
VTMGSLLFAI IASMVAWALI RNLPGLLEVL VLSRLNMRQG ASYAITTILN YIIIAVGAMT
VFGSLGVSWD KLQWLAAALS VGLGFGLQEI FGNFVSGLII LFERPVRIGD TVTIGSFSGT
VSKIRIRATT ITDFDRKEVI IPNKAFVTER LINWSLTDTT TRLVIRLGVA YGSDLEKVRK
VLLKAATEHP RVMHEPMPEV FFTAFGASTL DHELRLYVRE LRDRSRTVDE LNRTIDQLCR
ENDINIAFNQ LEVHLHNEKG DEVTEVKRDY KGDDPTPAVG
