TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.A.22.1.1









Large mechanosensitive ion channel: MscL; catalyzes efflux of ions (slightly cation selective), osmolytes and small proteins. Protein-lipid interactions are important for gating, dependent on TMS tilting (Iscla et al., 2011b).  The carboxyl-terminal cytoplasmic helices assemble into a pentameric bundle that resembles cartilage oligomeric matrix protein, and these are required for the selective formation of the pentamer (Ando et al. 2015). Lysophospholipids can increase the size of particles that can be transported (Foo et al. 2015).

Bacteria
Proteobacteria
MscL of E. coli (P0A742)
*1.A.22.1.2









Large mechanosensitive ion channel (3-D structure known)
Bacteria
Actinobacteria
MscL of Mycobacterium tuberculosis (P0A5K8)
*1.A.22.1.3









MscL; catalyzes ion and osmolyte release following osmmotic downshift
Bacteria
Firmicutes
MscL (YwpC) of Bacillus subtilis
*1.A.22.1.4









MscL (activated by arachidonate (Balleza et al., 2010), 45% identical to MscL of Bacillus subtilis (1.A.22.1.3)).

Bacteria
Proteobacteria
MscL of Rhizobium etli (Q2KCQ1)
*1.A.22.1.5









The pentameric MscL channel (Iscla et al., 2011).  The high resolution structure of a proposed closed but expanded tetrameric intermediate state has been determined (Liu et al. 2009).

Bacteria
Firmicutes
MscL of Staphylococcus aureus (P68805)
*1.A.22.1.6









MscL; rescues cells form osmotic downshift (Bucarey et al., 2012).

Bacteria
Actinobacteria
MscL of Micromonospora aurantica  (D9T6D3)
*1.A.22.1.7









Large-conductance mechanosensitive channel, MscL

Bacteria
Cyanobacteria
MscL of Synechococcus sp.
*1.A.22.1.8









Large-conductance mechanosensitive channel, MscL

Bacteria
Firmicutes
MscL of Leuconostoc citreum
*1.A.22.1.9









Large-conductance mechanosensitive channel, MscL

Bacteria
Actinobacteria
MscL of Renibacterium salmoninarum
*1.A.22.1.10









Osmotic adaptation channel that influences sporulation and secondary metabolite production, Sco3190 (MscL) (Wang et al. 2007).

Bacteria
Actinobacteria
Sco3190 of Streptomyces coelicolor
*1.A.22.1.11









Large conductance mechanosensitive channel protein, MscL, of 101 aas and 2 TMSs. When the membrane is stretched, MscL responds to the increase of membrane tension and opens a nonselective pore to about 30 A wide, exhibiting a large unitary conductance of approximately 3 nS. The structures of this archaeal MscL, trapped in the closed and expanded intermediate states, has been solved (Li et al. 2015). The comparative analysis of these two new structures reveals significant conformational rearrangements in the different domains of MscL. The large changes observed in the tilt angles of the two transmembrane helices (TMS1 and TMS2) fit well with the helix-pivoting model. Meanwhile, the periplasmic loop region transforms from a folded structure, containing an omega-shaped loop and a short beta-hairpin, to an extended and partly disordered conformation during channel expansion. Moreover, a significant rotating and sliding of the N-terminal helix (N-helix) is coupled to the tilting movements of TMS1 and TMS2. The dynamic relationships between the N-helix and TMS1/TMS2 suggest that the N-helix serves as a membrane-anchored stopper that limits the tilts of TM1 and TM2 in the gating process (Li et al. 2015).

Archaea
Euryarchaeota
MscL of Methanosarcina acetivorans
*1.A.22.1.12









MscL protein of 171 aas and 2 or 3 TMSs.

Eukaryota
Florideophyceae
MscL of Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa)