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Protein

Large-conductance mechanosensitive channel

Gene

mscL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell disruption and death. The force required to trigger channel opening depends on the membrane lipids composition.5 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • mechanosensitive ion channel activity Source: EcoCyc

GO - Biological processi

  • ion transmembrane transport Source: EcoCyc
  • ion transport Source: EcoliWiki

Keywordsi

Molecular functionIon channel
Biological processIon transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11180-MONOMER
MetaCyc:EG11180-MONOMER

Protein family/group databases

TCDBi1.A.22.1.1 the large conductance mechanosensitive ion channel (mscl) family

Names & Taxonomyi

Protein namesi
Recommended name:
Large-conductance mechanosensitive channelUniRule annotation
Gene namesi
Name:mscLUniRule annotation
Synonyms:yhdC
Ordered Locus Names:b3291, JW3252
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11180 mscL

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16CytoplasmicBy similarityAdd BLAST16
Transmembranei17 – 45HelicalBy similarityAdd BLAST29
Topological domaini46 – 74PeriplasmicBy similarityAdd BLAST29
Transmembranei75 – 94HelicalBy similarityAdd BLAST20
Topological domaini95 – 136CytoplasmicBy similarityAdd BLAST42

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49I → F or Y: Decreases the duration of the open state of the channel and decreases mechanosensitivity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001924391 – 136Large-conductance mechanosensitive channelAdd BLAST136

Proteomic databases

PaxDbiP0A742
PRIDEiP0A742

Interactioni

Subunit structurei

Homopentamer.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-909797,EBI-909797

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263415, 381 interactors
DIPiDIP-29827N
MINTiP0A742
STRINGi316385.ECDH10B_3465

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi117 – 134Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KYKmodel-A/B/C/D/E14-96[»]
1KYLmodel-A/B/C/D/E14-96[»]
1KYMmodel-A/B/C/D/E14-96[»]
4LKUX-ray1.45A/B/C/D/E108-136[»]
ProteinModelPortaliP0A742
SMRiP0A742
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The periplasmic loop between the two transmembrane domains modulates channel kinetics, and in particular the length of time the channel remains in the open conformation.1 Publication

Sequence similaritiesi

Belongs to the MscL family.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105M2E Bacteria
COG1970 LUCA
HOGENOMiHOG000226782
InParanoidiP0A742
KOiK03282
OMAiYGSFIQT
PhylomeDBiP0A742

Family and domain databases

Gene3Di1.10.1200.120, 1 hit
HAMAPiMF_00115 MscL, 1 hit
InterProiView protein in InterPro
IPR036019 Gated_MS_channel
IPR019823 Mechanosensitive_channel_CS
IPR001185 MS_channel
IPR037673 MSC/AndL
PANTHERiPTHR30266 PTHR30266, 1 hit
PfamiView protein in Pfam
PF01741 MscL, 1 hit
PRINTSiPR01264 MECHCHANNEL
SUPFAMiSSF81330 SSF81330, 1 hit
TIGRFAMsiTIGR00220 mscL, 1 hit
PROSITEiView protein in PROSITE
PS01327 MSCL, 1 hit

Sequencei

Sequence statusi: Complete.

P0A742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIIKEFREF AMRGNVVDLA VGVIIGAAFG KIVSSLVADI IMPPLGLLIG
60 70 80 90 100
GIDFKQFAVT LRDAQGDIPA VVMHYGVFIQ NVFDFLIVAF AIFMAIKLIN
110 120 130
KLNRKKEEPA AAPAPTKEEV LLTEIRDLLK EQNNRS
Length:136
Mass (Da):14,957
Last modified:June 7, 2005 - v1
Checksum:i18EF7E1BD7DF9491
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08371 Unassigned DNA Translation: AAA17745.1
L29458 Genomic DNA Translation: AAA24771.1
U18997 Genomic DNA Translation: AAA58088.1
U00096 Genomic DNA Translation: AAC76316.1
AP009048 Genomic DNA Translation: BAE78001.1
X52114 Genomic DNA Translation: CAA36360.1
PIRiI53826
RefSeqiNP_417749.1, NC_000913.3
WP_000022442.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76316; AAC76316; b3291
BAE78001; BAE78001; BAE78001
GeneIDi947787
KEGGiecj:JW3252
eco:b3291
PATRICifig|1411691.4.peg.3441

Entry informationi

Entry nameiMSCL_ECOLI
AccessioniPrimary (citable) accession number: P0A742
Secondary accession number(s): P23867, Q2M6V5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 28, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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