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DescriptionRecName: Full=Mechanosensitive channel MscK; AltName: Full=Potassium efflux system KefA; Flags: Precursor;
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MyHits synonymsMSCK_ECOLI , P77338 , Q2MBW2 , 809895660D2BD444
match map segment
ipat:UPF0003 ipfam:MS_channel ipfam:MscS_porin ipfam:MscS_TM  
Legends: 1, TOPO_DOM Periplasmic. {ECO:0000255}; 2, MUTAGEN G->S: Prevents growth in medium containing high levels of potassium in the presence of betaine. {ECO:0000269|PubMed:11985727}; 3, SIGNAL {ECO:0000255}; 4, TRANSMEM Helical. {ECO:0000255}; 5, TOPO_DOM Cytoplasmic. {ECO:0000255}; 6, COILED {ECO:0000255}; 7, ipat:UPF0003 [T].
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   02-NOV-2016, entry version 128.
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.,
RA   Mau B., 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
RT   MG1655 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.,
RA   Booth I.R.;
RT   "Protection of Escherichia coli cells against extreme turgor by
RT   activation of MscS and MscL mechanosensitive channels: identification
RT   of genes 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.,
RA   Epstein W., Booth I.R.;
RT   "Analysis of the kefA2 mutation suggests that KefA is a cation-
RT   specific 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
CC       membrane tension and specific ionic conditions. Requires high
CC       concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate.
CC       May participate in the regulation of osmotic pressure changes
CC       within the cell, although it does not appear to have a major role
CC       in osmolarity regulation. Forms an ion channel of 1.0 nanosiemens
CC       conductance. The channel can remain active for between 30 seconds
CC       and over 3 minutes; it does not desensitize upon extended
CC       pressure. Its activity is masked in wild-type cells by the MscS
CC       channel. {ECO:0000269|PubMed:10202137,
CC       ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:12374733}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:11985727, ECO:0000269|PubMed:15919996}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:11985727,
CC       ECO:0000269|PubMed:15919996}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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_LN832404.1.
DR   ProteinModelPortal; P77338; -.
DR   SMR; P77338; -.
DR   BioGrid; 4259842; 245.
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   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; 32116083; VBIEscCol129921_0483.
DR   EchoBASE; EB3991; -.
DR   EcoGene; EG14240; mscK.
DR   eggNOG; ENOG4105EGS; Bacteria.
DR   eggNOG; COG3264; LUCA.
DR   HOGENOM; HOG000280842; -.
DR   InParanoid; P77338; -.
DR   KO; K05802; -.
DR   OMA; LHTPKAI; -.
DR   PhylomeDB; P77338; -.
DR   BioCyc; EcoCyc:G6255-MONOMER; -.
DR   BioCyc; ECOL316407:JW0454-MONOMER; -.
DR   PRO; PR:P77338; -.
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:0009992; P:cellular water homeostasis; IMP:EcoCyc.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR010920; LSM_dom.
DR   InterPro; IPR011066; MscC_channel_C.
DR   InterPro; IPR006685; MscS_channel.
DR   InterPro; IPR006686; MscS_channel_CS.
DR   InterPro; IPR011014; MscS_channel_TM-2.
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; 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; Complete proteome;
KW   Ion transport; Membrane; Potassium; Potassium transport;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34   1120       Mechanosensitive channel MscK.
FT                                /FTId=PRO_0000043366.
FT   TOPO_DOM     34    499       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    500    520       Helical. {ECO:0000255}.
FT   TOPO_DOM    521    560       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    561    581       Helical. {ECO:0000255}.
FT   TOPO_DOM    582    582       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    583    603       Helical. {ECO:0000255}.
FT   TOPO_DOM    604    634       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    635    655       Helical. {ECO:0000255}.
FT   TOPO_DOM    656    657       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    658    678       Helical. {ECO:0000255}.
FT   TOPO_DOM    679    692       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    693    713       Helical. {ECO:0000255}.
FT   TOPO_DOM    714    728       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    729    749       Helical. {ECO:0000255}.
FT   TOPO_DOM    750    796       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    797    817       Helical. {ECO:0000255}.
FT   TOPO_DOM    818    839       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    840    860       Helical. {ECO:0000255}.
FT   TOPO_DOM    861    886       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    887    907       Helical. {ECO:0000255}.
FT   TOPO_DOM    908    921       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    922    942       Helical. {ECO:0000255}.
FT   TOPO_DOM    943   1120       Cytoplasmic. {ECO:0000255}.
FT   COILED       43     98       {ECO:0000255}.
FT   COILED      126    266       {ECO:0000255}.
FT   COILED      360    422       {ECO:0000255}.
FT   COILED     1057   1081       {ECO:0000255}.
FT   MUTAGEN     922    922       G->S: Prevents growth in medium
FT                                containing high levels of potassium in
FT                                the presence of betaine.
FT                                {ECO:0000269|PubMed:11985727}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       959    993       ipat:UPF0003 [T]
FT   MYHIT       887   1086       ipfam:MS_channel [T]
FT   MYHIT        50    289       ipfam:MscS_porin [T]
FT   MYHIT       509    826       ipfam:MscS_TM [T]
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
//