MSCL_MYCTU
ID MSCL_MYCTU Reviewed; 151 AA.
AC P9WJN5; L0T5D5; O53898; P0A5K8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=Rv0985c;
GN ORFNames=MTV044.13c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23875651; DOI=10.1021/bi400790j;
RA Zhong D., Blount P.;
RT "Phosphatidylinositol is crucial for the mechanosensitivity of
RT Mycobacterium tuberculosis MscL.";
RL Biochemistry 52:5415-5420(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 10-118, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9856938; DOI=10.1126/science.282.5397.2220;
RA Chang G., Spencer R.H., Lee A.T., Barclay M.T., Rees D.C.;
RT "Structure of the MscL homolog from Mycobacterium tuberculosis: a gated
RT mechanosensitive ion channel.";
RL Science 282:2220-2226(1998).
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:0000269|PubMed:23875651}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:9856938}.
CC -!- INTERACTION:
CC P9WJN5; P9WJN5: mscL; NbExp=2; IntAct=EBI-15799854, EBI-15799854;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:23875651, ECO:0000305|PubMed:9856938}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00115,
CC ECO:0000269|PubMed:9856938}.
CC -!- MISCELLANEOUS: E.coli inner membranes are often used to measure the
CC activity of heterologously expressed channels, but the lipid
CC composition of E.coli membranes differs considerably from that of
CC M.tuberculosis. Phosphatidylinositol is one of the major constituents
CC of M.tuberculosis membranes, but not of E.coli membranes, and this
CC affects channel activity. {ECO:0000269|PubMed:23875651}.
CC -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC Rule:MF_00115, ECO:0000305}.
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DR EMBL; AL123456; CCP43735.1; -; Genomic_DNA.
DR PIR; E70821; E70821.
DR RefSeq; NP_215500.1; NC_000962.3.
DR RefSeq; WP_003405128.1; NZ_NVQJ01000018.1.
DR PDB; 2OAR; X-ray; 3.50 A; A/B/C/D/E=1-151.
DR PDB; 6CTD; X-ray; 5.80 A; A/B/C/D/E/F/G/H/I/J=1-101.
DR PDBsum; 2OAR; -.
DR PDBsum; 6CTD; -.
DR AlphaFoldDB; P9WJN5; -.
DR SMR; P9WJN5; -.
DR STRING; 83332.Rv0985c; -.
DR PaxDb; P9WJN5; -.
DR DNASU; 885368; -.
DR GeneID; 885368; -.
DR KEGG; mtu:Rv0985c; -.
DR TubercuList; Rv0985c; -.
DR eggNOG; COG1970; Bacteria.
DR OMA; AWIIFLM; -.
DR PhylomeDB; P9WJN5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0022836; F:gated channel activity; IDA:MTBBASE.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:MTBBASE.
DR GO; GO:0009992; P:cellular water homeostasis; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IDA:MTBBASE.
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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..151
FT /note="Large-conductance mechanosensitive channel"
FT /id="PRO_0000192452"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9856938"
FT TRANSMEM 15..43
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9856938"
FT TOPO_DOM 44..68
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9856938"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9856938"
FT TOPO_DOM 90..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9856938"
FT REGION 122..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:2OAR"
FT HELIX 13..46
FT /evidence="ECO:0007829|PDB:2OAR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2OAR"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2OAR"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:2OAR"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:2OAR"
FT HELIX 106..123
FT /evidence="ECO:0007829|PDB:2OAR"
SQ SEQUENCE 151 AA; 16023 MW; D682D3F2C1651E9C CRC64;
MLKGFKEFLA RGNIVDLAVA VVIGTAFTAL VTKFTDSIIT PLINRIGVNA QSDVGILRIG
IGGGQTIDLN VLLSAAINFF LIAFAVYFLV VLPYNTLRKK GEVEQPGDTQ VVLLTEIRDL
LAQTNGDSPG RHGGRGTPSP TDGPRASTES Q
