MSCL_MYCTA
ID MSCL_MYCTA Reviewed; 151 AA.
AC A5U127;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=MRA_0992;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
CC -!- FUNCTION: Channel that opens in response to stretch forces in the
CC membrane lipid bilayer. The force required to trigger channel opening
CC depends on the nature of the membrane lipids; the presence of
CC phosphatidylinositol enhances mechanosensitivity of the channel. May
CC participate in the regulation of osmotic pressure changes within the
CC cell. {ECO:0000250|UniProtKB:P9WJN5}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000250|UniProtKB:P9WJN5,
CC ECO:0000255|HAMAP-Rule:MF_00115}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WJN5,
CC ECO:0000255|HAMAP-Rule:MF_00115}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P9WJN5, 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; CP000611; ABQ72727.1; -; Genomic_DNA.
DR RefSeq; WP_003405128.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U127; -.
DR SMR; A5U127; -.
DR STRING; 419947.MRA_0992; -.
DR EnsemblBacteria; ABQ72727; ABQ72727; MRA_0992.
DR KEGG; mra:MRA_0992; -.
DR eggNOG; COG1970; Bacteria.
DR HOGENOM; CLU_095787_1_1_11; -.
DR OMA; AWIIFLM; -.
DR OrthoDB; 1863650at2; -.
DR EvolutionaryTrace; A5U127; -.
DR Proteomes; UP000001988; 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; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..151
FT /note="Large-conductance mechanosensitive channel"
FT /id="PRO_0000300062"
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..68
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT TOPO_DOM 90..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WJN5"
FT REGION 122..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 16023 MW; D682D3F2C1651E9C CRC64;
MLKGFKEFLA RGNIVDLAVA VVIGTAFTAL VTKFTDSIIT PLINRIGVNA QSDVGILRIG
IGGGQTIDLN VLLSAAINFF LIAFAVYFLV VLPYNTLRKK GEVEQPGDTQ VVLLTEIRDL
LAQTNGDSPG RHGGRGTPSP TDGPRASTES Q