MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Mechanosensitive channel MscK; AltName: Full=Potassium efflux system KefA; Flags: Precursor; |
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| MyHits synonyms | MSCK_ECOLI , P77338 , Q2MBW2 , 809895660D2BD444 |
 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].
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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 887 1086 ipfam:MS_channel [T]
FT MYHIT 50 289 ipfam:MscS_porin [T]
FT MYHIT 959 993 ipat:UPF0003 [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
//
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