ID   MSCL_STAAW              Reviewed;         120 AA.
AC   P68806; O68285;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN   Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=MW1235;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
RN   [2] {ECO:0007744|PDB:3HZQ}
RP   X-RAY CRYSTALLOGRAPHY (3.82 ANGSTROMS) OF 1-94, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=19701184; DOI=10.1038/nature08277;
RA   Liu Z., Gandhi C.S., Rees D.C.;
RT   "Structure of a tetrameric MscL in an expanded intermediate state.";
RL   Nature 461:120-124(2009).
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 3 nanosiemens. May participate in the regulation
CC       of osmotic pressure changes within the cell.
CC       {ECO:0000269|PubMed:19701184}.
CC   -!- SUBUNIT: Homopentamer (By similarity). Can form a homotetramer (in
CC       vitro), but this may not be physiologically relevant (PubMed:19701184).
CC       {ECO:0000250|UniProtKB:Q6G9L1, ECO:0000255|HAMAP-Rule:MF_00115,
CC       ECO:0000269|PubMed:19701184}.
CC   -!- INTERACTION:
CC       P68806; P68806: mscL; NbExp=3; IntAct=EBI-15799893, EBI-15799893;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115,
CC       ECO:0000305|PubMed:19701184}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000305|PubMed:19701184}.
CC   -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC       Rule:MF_00115, ECO:0000305}.
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DR   EMBL; BA000033; BAB95100.1; -; Genomic_DNA.
DR   RefSeq; WP_000910489.1; NC_003923.1.
DR   PDB; 3HZQ; X-ray; 3.82 A; A=1-94.
DR   PDBsum; 3HZQ; -.
DR   AlphaFoldDB; P68806; -.
DR   SMR; P68806; -.
DR   DIP; DIP-59298N; -.
DR   EnsemblBacteria; BAB95100; BAB95100; BAB95100.
DR   KEGG; sam:MW1235; -.
DR   HOGENOM; CLU_095787_0_0_9; -.
DR   OMA; AWIIFLM; -.
DR   EvolutionaryTrace; P68806; -.
DR   Proteomes; UP000000418; Chromosome.
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   3D-structure; Cell membrane; Ion channel; Ion transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..120
FT                   /note="Large-conductance mechanosensitive channel"
FT                   /id="PRO_0000192466"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:19701184"
FT   TRANSMEM        15..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000305|PubMed:19701184"
FT   TOPO_DOM        44..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:19701184"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000305|PubMed:19701184"
FT   TOPO_DOM        83..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:19701184"
SQ   SEQUENCE   120 AA;  13616 MW;  A4D1E6B2A7B7D2E5 CRC64;
     MLKEFKEFAL KGNVLDLAIA VVMGAAFNKI ISSLVENIIM PLIGKIFGSV DFAKEWSFWG
     IKYGLFIQSV IDFIIIAFAL FIFVKIANTL MKKEEAEEEA VVEENVVLLT EIRDLLREKK