MSCL_ECOLI
ID MSCL_ECOLI Reviewed; 136 AA.
AC P0A742; P23867; Q2M6V5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; Synonyms=yhdC;
GN OrderedLocusNames=b3291, JW3252;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-37, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7511799; DOI=10.1038/368265a0;
RA Sukharev S.I., Blount P., Martinac B., Blattner F.R., Kung C.;
RT "A large-conductance mechanosensitive channel in E. coli encoded by mscL
RT alone.";
RL Nature 368:265-268(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8063098; DOI=10.1016/0378-1119(94)90847-8;
RA Christie G.E., White T.J., Goodwin T.S.;
RT "A merR homologue at 74 minutes on the Escherichia coli genome.";
RL Gene 146:131-132(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=8412700; DOI=10.1111/j.1365-2958.1993.tb01714.x;
RA Schloesser A., Hamann A., Bossemeyer D., Schneider E., Bakker E.P.;
RT "NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence
RT similarity between TrkA and domains of a family of dehydrogenases suggest a
RT role for NAD+ in bacterial transport.";
RL Mol. Microbiol. 9:533-543(1993).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
RX PubMed=8890153; DOI=10.1002/j.1460-2075.1996.tb00860.x;
RA Blount P., Sukharev S.I., Moe P.C., Schroeder M.J., Guy H.R., Kung C.;
RT "Membrane topology and multimeric structure of a mechanosensitive channel
RT protein of Escherichia coli.";
RL EMBO J. 15:4798-4805(1996).
RN [7]
RP SUBUNIT, AND REVISION OF SUBUNIT NUMBER.
RX PubMed=9856938; DOI=10.1126/science.282.5397.2220;
RA Chang G., Spencer R.H., Lee A.T., Barclay M.T., Rees D.C.;
RT "Structure of the MscL homolog from Mycobacterium tuberculosis: a gated
RT mechanosensitive ion channel.";
RL Science 282:2220-2226(1998).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9632260; DOI=10.1046/j.1365-2958.1998.00821.x;
RA Moe P.C., Blount P., Kung C.;
RT "Functional and structural conservation in the mechanosensitive channel
RT mscL implicates elements crucial for mechanosensation.";
RL Mol. Microbiol. 28:583-592(1998).
RN [9]
RP FUNCTION, AND PHYSIOLOGICAL ROLE.
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 [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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).
RN [11]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21151884; DOI=10.1371/journal.pbio.1000555;
RA Dorwart M.R., Wray R., Brautigam C.A., Jiang Y., Blount P.;
RT "S. aureus MscL is a pentamer in vivo but of variable stoichiometries in
RT vitro: implications for detergent-solubilized membrane proteins.";
RL PLoS Biol. 8:E1000555-E1000555(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23875651; DOI=10.1021/bi400790j;
RA Zhong D., Blount P.;
RT "Phosphatidylinositol is crucial for the mechanosensitivity of
RT Mycobacterium tuberculosis MscL.";
RL Biochemistry 52:5415-5420(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ILE-49.
RX PubMed=23416054; DOI=10.1016/j.celrep.2013.01.018;
RA Yang L.M., Zhong D., Blount P.;
RT "Chimeras reveal a single lipid-interface residue that controls MscL
RT channel kinetics as well as mechanosensitivity.";
RL Cell Rep. 3:520-527(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 108-136, AND SUBUNIT.
RX PubMed=24038743; DOI=10.1002/pro.2360;
RA Walton T.A., Rees D.C.;
RT "Structure and stability of the C-terminal helical bundle of the E. coli
RT mechanosensitive channel of large conductance.";
RL Protein Sci. 22:1592-1601(2013).
CC -!- FUNCTION: Mechanosensitive channel that opens in response to stretch
CC forces in the membrane lipid bilayer. Forms a nonselective ion channel
CC with a conductance of about 4 nanosiemens. Participates in the
CC regulation of osmotic pressure changes within the cell. Opens at a
CC pressure just below that which would cause cell disruption and death.
CC The force required to trigger channel opening depends on the membrane
CC lipids composition. {ECO:0000269|PubMed:10202137,
CC ECO:0000269|PubMed:23416054, ECO:0000269|PubMed:23875651,
CC ECO:0000269|PubMed:7511799, ECO:0000269|PubMed:9632260}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:21151884, ECO:0000269|PubMed:24038743,
CC ECO:0000269|PubMed:8890153, ECO:0000269|PubMed:9856938}.
CC -!- INTERACTION:
CC P0A742; P0A742: mscL; NbExp=6; IntAct=EBI-909797, EBI-909797;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00115, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:23416054, ECO:0000269|PubMed:7511799,
CC ECO:0000269|PubMed:8890153, ECO:0000269|PubMed:9632260,
CC ECO:0000305|PubMed:21151884, ECO:0000305|PubMed:23875651}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8890153}.
CC -!- DOMAIN: The periplasmic loop between the two transmembrane domains
CC modulates channel kinetics, and in particular the length of time the
CC channel remains in the open conformation.
CC {ECO:0000269|PubMed:23416054}.
CC -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC Rule:MF_00115, ECO:0000305}.
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DR EMBL; U08371; AAA17745.1; -; Unassigned_DNA.
DR EMBL; L29458; AAA24771.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58088.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76316.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78001.1; -; Genomic_DNA.
DR EMBL; X52114; CAA36360.1; -; Genomic_DNA.
DR PIR; I53826; I53826.
DR RefSeq; NP_417749.1; NC_000913.3.
DR RefSeq; WP_000022442.1; NZ_STEB01000038.1.
DR PDB; 4LKU; X-ray; 1.45 A; A/B/C/D/E=108-136.
DR PDBsum; 4LKU; -.
DR AlphaFoldDB; P0A742; -.
DR SMR; P0A742; -.
DR BioGRID; 4263415; 381.
DR DIP; DIP-29827N; -.
DR MINT; P0A742; -.
DR STRING; 511145.b3291; -.
DR TCDB; 1.A.22.1.1; the large conductance mechanosensitive ion channel (mscl) family.
DR jPOST; P0A742; -.
DR PaxDb; P0A742; -.
DR PRIDE; P0A742; -.
DR EnsemblBacteria; AAC76316; AAC76316; b3291.
DR EnsemblBacteria; BAE78001; BAE78001; BAE78001.
DR GeneID; 60902085; -.
DR GeneID; 947787; -.
DR KEGG; ecj:JW3252; -.
DR KEGG; eco:b3291; -.
DR PATRIC; fig|1411691.4.peg.3441; -.
DR EchoBASE; EB1167; -.
DR eggNOG; COG1970; Bacteria.
DR HOGENOM; CLU_095787_0_0_6; -.
DR InParanoid; P0A742; -.
DR OMA; AWIIFLM; -.
DR PhylomeDB; P0A742; -.
DR BioCyc; EcoCyc:EG11180-MON; -.
DR BioCyc; MetaCyc:EG11180-MON; -.
DR PRO; PR:P0A742; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:EcoCyc.
DR GO; GO:0009992; P:cellular water homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006811; P:ion transport; IDA:EcoliWiki.
DR Gene3D; 1.10.1200.120; -; 1.
DR HAMAP; MF_00115; MscL; 1.
DR InterPro; IPR019823; Mechanosensitive_channel_CS.
DR InterPro; IPR001185; MS_channel.
DR InterPro; IPR037673; MSC/AndL.
DR InterPro; IPR036019; MscL_channel.
DR PANTHER; PTHR30266; PTHR30266; 1.
DR Pfam; PF01741; MscL; 1.
DR PRINTS; PR01264; MECHCHANNEL.
DR SUPFAM; SSF81330; SSF81330; 1.
DR TIGRFAMs; TIGR00220; mscL; 1.
DR PROSITE; PS01327; MSCL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..136
FT /note="Large-conductance mechanosensitive channel"
FT /id="PRO_0000192439"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TRANSMEM 17..45
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TOPO_DOM 46..74
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TOPO_DOM 95..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT MUTAGEN 49
FT /note="I->F,Y: Decreases the duration of the open state of
FT the channel and decreases mechanosensitivity."
FT /evidence="ECO:0000269|PubMed:23416054"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:4LKU"
SQ SEQUENCE 136 AA; 14957 MW; 18EF7E1BD7DF9491 CRC64;
MSIIKEFREF AMRGNVVDLA VGVIIGAAFG KIVSSLVADI IMPPLGLLIG GIDFKQFAVT
LRDAQGDIPA VVMHYGVFIQ NVFDFLIVAF AIFMAIKLIN KLNRKKEEPA AAPAPTKEEV
LLTEIRDLLK EQNNRS
