MSCL_CLOPE
ID MSCL_CLOPE Reviewed; 152 AA.
AC P53380; P54747;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=CPE0174;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
RX PubMed=7489908; DOI=10.1016/0378-1119(95)00490-w;
RA Matsushita O., Jung C.M., Okabe A.;
RT "Identification of the gene encoding a mechanosensitive channel MscL
RT homologue in Clostridium perfringens.";
RL Gene 165:147-148(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00115}.
CC -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC Rule:MF_00115, ECO:0000305}.
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DR EMBL; D50309; BAA08847.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79880.1; -; Genomic_DNA.
DR RefSeq; WP_011009654.1; NC_003366.1.
DR AlphaFoldDB; P53380; -.
DR SMR; P53380; -.
DR STRING; 195102.gene:10489418; -.
DR EnsemblBacteria; BAB79880; BAB79880; BAB79880.
DR KEGG; cpe:CPE0174; -.
DR HOGENOM; CLU_095787_2_3_9; -.
DR OMA; AWIIFLM; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cell membrane; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..152
FT /note="Large-conductance mechanosensitive channel"
FT /id="PRO_0000192438"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
FT CONFLICT 22
FT /note="I -> V (in Ref. 1; BAA08847)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="I -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="R -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> V (in Ref. 1; BAA08847)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="Q -> K (in Ref. 1; BAA08847)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="C -> Y (in Ref. 1; BAA08847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 16811 MW; 528E9236BF45C87F CRC64;
MWKEFKEFAM KGNVIDLAIG VIIGGAFGKI VTSLVNDIIM PVIGRLVGKV DFSNLYINLS
GQQFNSLQEA QAAGAATINY GLFLNNLINF LIIAFSIFIA IKQINKLKNF TKKKEEVQVE
ATEKDCPYCC TKIDIKATRC PHCTSVLEEA TN