MSCL_STAAS
ID MSCL_STAAS Reviewed; 120 AA.
AC Q6G9L1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=SAS1287;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
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).
CC -!- FUNCTION: Channel that opens in response to stretch forces in the
CC membrane lipid bilayer. May participate in the regulation of osmotic
CC pressure changes within the cell. {ECO:0000255|HAMAP-Rule:MF_00115}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:21151884}.
CC -!- INTERACTION:
CC Q6G9L1; Q6G9L1: mscL; NbExp=6; IntAct=EBI-15898345, EBI-15898345;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:21151884}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00115}.
CC -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC Rule:MF_00115}.
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DR EMBL; BX571857; CAG43065.1; -; Genomic_DNA.
DR RefSeq; WP_000910489.1; NC_002953.3.
DR AlphaFoldDB; Q6G9L1; -.
DR SMR; Q6G9L1; -.
DR DIP; DIP-58957N; -.
DR KEGG; sas:SAS1287; -.
DR HOGENOM; CLU_095787_0_0_9; -.
DR OMA; AWIIFLM; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IEA:UniProtKB-UniRule.
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 Cell membrane; Ion channel; Ion transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..120
FT /note="Large-conductance mechanosensitive channel"
FT /id="PRO_0000192464"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
SQ SEQUENCE 120 AA; 13616 MW; A4D1E6B2A7B7D2E5 CRC64;
MLKEFKEFAL KGNVLDLAIA VVMGAAFNKI ISSLVENIIM PLIGKIFGSV DFAKEWSFWG
IKYGLFIQSV IDFIIIAFAL FIFVKIANTL MKKEEAEEEA VVEENVVLLT EIRDLLREKK