ID   MSCL_STAA8              Reviewed;         120 AA.
AC   P68805; O68285;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN   Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115};
GN   OrderedLocusNames=SAOUHSC_01345;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-47.
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).
CC   -!- FUNCTION: Channel that opens in response to stretch forces in the
CC       membrane lipid bilayer. Forms a nonselective ion channel with a
CC       conductance of about 2.5-4 nanosiemens. May participate in the
CC       regulation of osmotic pressure changes within the cell.
CC       {ECO:0000269|PubMed:23416054, ECO:0000269|PubMed:9632260}.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000250|UniProtKB:Q6G9L1,
CC       ECO:0000255|HAMAP-Rule:MF_00115}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115,
CC       ECO:0000305|PubMed:23416054, ECO:0000305|PubMed:9632260}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P68806, ECO:0000255|HAMAP-
CC       Rule:MF_00115}.
CC   -!- DOMAIN: The extracellular 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; AF029731; AAC38560.1; -; Genomic_DNA.
DR   EMBL; CP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_000910489.1; NZ_LS483365.1.
DR   RefSeq; YP_008530241.1; NC_007795.1.
DR   AlphaFoldDB; P68805; -.
DR   SMR; P68805; -.
DR   STRING; 1280.SAXN108_1364; -.
DR   TCDB; 1.A.22.1.5; the large conductance mechanosensitive ion channel (mscl) family.
DR   GeneID; 16830701; -.
DR   KEGG; sao:SAOUHSC_1342a; -.
DR   eggNOG; COG1970; Bacteria.
DR   PRO; PR:P68805; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR   GO; GO:0009992; P:cellular water homeostasis; IBA:GO_Central.
DR   GO; GO:0006811; P:ion transport; IBA:GO_Central.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..120
FT                   /note="Large-conductance mechanosensitive channel"
FT                   /id="PRO_0000192465"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT   TRANSMEM        15..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT   TOPO_DOM        44..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT   TOPO_DOM        83..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT   MUTAGEN         47
FT                   /note="F->E,K: Decreases the duration of the open state of
FT                   the channel. Increases mechanosensitivity."
FT                   /evidence="ECO:0000269|PubMed:23416054"
FT   MUTAGEN         47
FT                   /note="F->I,L: Increases the duration of the open state of
FT                   the channel."
FT                   /evidence="ECO:0000269|PubMed:23416054"
SQ   SEQUENCE   120 AA;  13616 MW;  A4D1E6B2A7B7D2E5 CRC64;
     MLKEFKEFAL KGNVLDLAIA VVMGAAFNKI ISSLVENIIM PLIGKIFGSV DFAKEWSFWG
     IKYGLFIQSV IDFIIIAFAL FIFVKIANTL MKKEEAEEEA VVEENVVLLT EIRDLLREKK