1.A.23 The Small Conductance Mechanosensitive Ion Channel (MscS) Family

The MscS family (the SwissProt UPF0003 family) is a group of topographically diverse proteins, some of which are functionally characterized. They exhibit homology in only a restricted region. Early electrophysiological studies with E. coli suggested the presence of two distinguishable mechanosensitive ion channels, one with large conductance (MscL; TC #1.A.22) and one with small conductance (MscS; this family) (Martinac et al., 1987, 1990). Cytoplasmic beta domains appear to be new gating elements in MscS channels (Koprowski et al., 2011).  Open and closed conformational states of the heptameric channel have been proposed and discussed (Pliotas et al. 2012). Evolutionary considerations have been reported (Booth et al. 2015).  Some MscS channels may function in amino acid efflux, Ca2+ regulation and cell division (Cox et al. 2015). Mechanosensitive MscS channels can be gated by delipidation (Flegler et al. 2021).

Application of a ramp of negative pressure to a patch excised from an E. coli giant spheroplast gave (1) a small conductance (MscS; ~1 nS in 400 mM salt) with a sustained open state, and (2) a large conductance (MscL; ~3 nS) with faster kinetics, activated at higher pressure. MscS was reported to exhibit a weak anionic preference and a voltage dependency, tending to open upon depolarization. Activation by membrane-intercalating amphipathic compounds suggested that the MscS channel is sensitive to mechanical perturbations in the lipid bilayer. It was suggested that MscS plays a role in fast osmoregulatory responses. How these channels may respond to change in the mechanical environment the lipid bilayer provides is discussed by Kung et al. (2010). Mechanosensitive ion channels have been discussed in terms of their physiological importance and their potential roles in cancer (Otero-Sobrino et al. 2023).

Mechanosensitive channels function as electromechanical switches with the capability to sense the physical state of lipid bilayers. The X-ray crystal structures of MscL and MscS allow identification of the types of protein motions associated with the opening and closing of these structurally unrelated channels, while providing the framework to address a mechanism of tension sensing that is defined by channel-lipid interactions (Perozo and Rees, 2003). Functional, structural and dynamic data offer fresh insights into the molecular basis of gating for these membrane proteins.  Members of the MscS family are found in bacteria, archaea, fungi, and plants (Wilson et al. 2013). Differential expression of various mscS genes in tissue developmental stages and under stress conditions in plants suggested roles in development and stress responses. Altered expression during CaCl2 stress suggested a role in Ca2+ homeostasis, signaling, growth, and defense responses (Kaur et al. 2020).

Mutations in the genes encoding the KefA (AefA) and YggB proteins of E. coli block the MscS mechanosensitive channel activity. The principal one is affected by knockouts of YggB, while the minor one is affected by knockouts of KefA. These two channels open in response to pressure changes during osmotic downshift just below those that cause cell disruption and death (Biggin and Sansom, 2003; Pivetti et al., 2003). The C-termini of the YggB heptameric channel move apart upon channel opening and may serve as the gate (Koprowski and Kubalski, 2003). High resolution 3-D structures are available (Bass et al., 2002; Lai et al. 2013). Crosslinking studies indicate that a large conformational change accompanies the open to the closed configuration (Miller et al., 2003b).

Homologues of YggB are found in Gram-negative, Gram-positive and cyanobacteria, in archaea, in yeast and in plants, but not in animals (Booth and Louis, 1999). One archaeon, Haloferax volcanii, exhibits mechanosensitive channels similar in conductance and mass to YggB of E. coli, but the sequences of these channel proteins are not available (Le Dain et al., 1998). Two sequenced MscS homologues have been functionally characterized from Methanococcus jannaschii (Kloda and Martinac, 2001a,b).

MscS family homologues vary in length between 248 and 1120 amino acyl residues, but the homologous region that is shared by most of them is only 200-250 residues long, exhibiting 4-5 TMSs (Miller et al., 2003b). The topologies of these proteins differ drastically. YggB (286 aas; spP11666) exhibits 4-5 putative transmembrane α-helical spanners (TMSs); KefA (AefA) (1120 aas; spP77338) exhibits 11 TMSs; YjeP of E. coli (1107 aas; spP39285) exhibits 11 TMSs; YbiO of E. coli (741 aas; spP75783) exhibits 10 TMSs; and YbdG of E. coli (415 aas; spP39455) exhibits 5 TMSs. Moreover, of the M. jannaschii homologues, MJ0170 (350 aas; spQ57634) exhibits 4-5 TMSs; MJ0700 (324 aas; spQ58111) exhibits 4 TMSs; and MJ1143 (361 aas; spQ58543) exhibits 5-6 TMSs. This topological variability is an unusual characteristic of a family of homologous transport proteins, and its functional significance cannot be evaluated at this time. It is possible that transport mechanisms will vary in accordance with topology. On the other hand, only 2 TMSs, common to all of these proteins may comprise the channel (Booth and Louis, 1999).

The E. coli and Synechocystis genomes include five recognized paralogues of the MscS family while the Bacillus subtilis and Methanococcus jannaschii genomes include three paralogues. KefA is multidomain and may be multifunctional. It has a large (470 amino acyl residues) N-terminal extracytoplasmic domain that may interact with the peptidoglycan cell wall, a central hydrophobic region including the 11 TMSs (residues 480-940), and a C-terminal cytoplasmic domain (residues 941-1120). Only the last four TMSs and the C-terminal hydrophilic domain are homologous to the much shorter YggA protein. One of the Synechocystis homologues (slr1575) possesses a C-terminal domain homologous to cyclic AMP-dependent protein kinaseA regulatory subunits (Ochoa de Alde and Houmard, 2000). It may therefore be a cyclic nucleotide-regulated channel.

A homologue of MscS channels in Erwinia chrysanthemi, BspA, is encoded within an operon that includes the psd gene encoding phosphatidyl serine decarboxylase. In high salts medium, glycine betaine initially is taken up normally in a bspA mutant, but uptake is followed by reduced glucose uptake and release of glycine betaine without loss of viability. It was suggested that BspA is not a channel but instead senses the intracellular glycine betaine and the extracellular salt concentrations, and thus serves as a receptor for osmoadaptation (Touzé et al., 2001).

In bacterial and animal systems, mechanosensitive (MS) ion channels are thought to mediate the perception of pressure, touch, and sound. Ten MscS-Like (MSL) proteins are encoded within the genome of Arabidopsis thaliana. MSL2 and MSL3, along with MSC1, a MscS family member from green algae, are implicated in the control of organelle morphology. Haswell et al. (2008) characterized MSL9 and MSL10, two MSL proteins found in the plasma membrane of root cells. MSL9 and MSL10, along with three other members of the MSL family, are required for MS channel activities detected in protoplasts derived from root cells.

The Escherichia coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. Wang et al. (2008) described a 3.45 angstrom-resolution structure in an open conformation. MscS has a pore diameter of ~13 angstroms created by substantial rotational rearrangement of the three transmembrane helices. The structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation (Wang et al., 2008). The levels of both MscL and MscS channels in Bacillus subtilis are high during exponential phase growth, very low in stationary phase and non-detectable in spores (Wahome et al., 2009). 

The E. coli MscS (EcMscS) has been extensively studied, but it may display characteristics not widely conserved in this protein family. With numerous members now electrophysiologically characterized, these channels displays a breadth of ion selectivity with both anion and cation selective members. The selectivities of these channels may be relatively weak in comparison to voltage-gated channels. Residues important for selectivity in MscS homologs suggest different selectivity mechanisms than those employed by voltage gated K+, Na+, Ca2+ and Cl- channels whose selectivity filters are housed within their transmembrane pores. Cox et al. 2013 attempted to unravel the potential physiological relevance of these differences. 

Mechanosensitive (MS) channels provide protection against hypo-osmotic shock in bacteria whereas eukaryotic MS channels fulfill a multitude of important functions in addition to osmoregulation. Interactions with the membrane lipids are responsible for the sensing of mechanical force for most known MS channels. Not only prokaryotic, but also eukaryotic, MS channels are able to directly sense the tension in the membrane bilayer without an additional cofactor. Sensitivity towards tension changes can be explained as result of the hydrophobic coupling between membrane and transmembrane (TM) regions of the channel. Molecular interactions of lipids with the channels may play an important role in mechanosensation. Pockets in between TM helices were identified in MscS and YnaI (TC# 1.A.23.4.3) that are filled with lipids. Fewer lipids are present in the open state of MscS than the closed. Thus, exclusion of lipid fatty acyl chains from these pockets, as a consequence of increased tension, may trigger gating. Similarly, in the eukaryotic MS channel TRAAK it was found that a lipid chain blocks the conducting path in the closed state (Rasmussen 2016).

The generalized transport reaction proposed for MscS channels is:

osmolytes (in) and ions (in) osmolytes (out) and ions (out).



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TC#NameOrganismal TypeExample

Minor K+-dependent MscS-type mechanosensitive channel protein, designated KefA, AefA or MscK, (Edwards et al. 2012). 

Bacteria, archaea, yeast, plants

KefA (AefA) of E. coli

1.A.23.1.2The putative osmoadaptation receptor, BspABacteriaBspA of Erwinia (Pectobacterium) chrysanthemi

Mini conductance (300 pS) mechanosensitive channel, YjeP or MscM (1107aas; 13 TMSs in a 1 + 12 TMS arrangement).  Encoded in an operon with phosphatidyl serine decarboxylase (Moraes and Reithmeier 2012). Protects against hypoosmotic shock (Edwards et al. 2012).


YjeP of E. coli (P39285)


Uncharacterized protein of 571 aas and 6 TMSs.

UP of Bdellovibrio exovorus


Mechanosensitive ion channel, MscS, of 952 aas and 10 TMSs.

MscS of Legionella sp.


TC#NameOrganismal TypeExample

Major MscS channel protein, YggB. Seven residues, mostly hydrophobic, in the first and second transmembrane helices are lipid-sensing residues (Malcolm et al., 2011).  X-ray structures are available (Lai et al. 2013).  The cytoplasmic cage domain senses macromolecular crowding (Rowe et al. 2014). A gating mechanism has been proposed (Malcolm et al. 2015).  The thermodynamics of K+ leak have been studied (Koprowski et al. 2015).  In the MscS crystal structure (PDB 2OAU ), a narrow, hydrophobic opening is visible in the crystal structure, and a vapor lock, created by hydrophobic seals consisting of L105 and L109, is the barrier to water and ions (Rasmussen et al. 2015). The voltage dependence of inactivation occurs independently of the positive charges of R46, R54, and R74 (Nomura et al. 2016). The closed-to-open transition may involve rotation and tilt of the pore-lining helices (Edwards et al. 2005). A molecular dynamics study of gating has been published (Sotomayor and Schulten 2004). It suggested that when restraining the backbone of the protein, the channel remained in the open form and the simulation revealed intermittent permeation of water molecules through the channel. Abolishing the restraints under constant pressure conditions led to spontaneous closure of the transmembrane channel, whereas abolishing the restraints when surface tension (20 dyn/cm) was applied led to channel widening. The large balloon-shaped cytoplasmic domain of MscS exhibited spontaneous diffusion of ions through its side openings. Interaction between the transmembrane domain and the cytoplasmic domain of MscS was observed and involved formation of salt bridges between residues Asp62 and Arg128; this interaction may be essential for the gating of MscS. K+ and Cl- ions showed distinctively different distributions in and around the channel (Sotomayor and Schulten 2004).

Protobacteria; homologues are found in archaea, yeast and plants.

YggB or MscS of E. coli (P0C0S1)


MscS protein.  The x-ray structure at 4.2 Å is available (Lai et al. 2013).


MscS of Helicobacter pylori


MscS mechanosensitive channel of 462 aas and 5 TMSs.

MscS channel of Candidatus Peribacter riflensis


Putative small conductance mechanosensetive channel protein of 261 aas and 3 TMSs

MscS homologue of Aureococcus anophagefferens virus


TC#NameOrganismal TypeExample
1.A.23.3.1The YkuT osmolyte efflux channel Bacteria, archaea, yeast, plants YkuT of Bacillus subtilis

Mechanosensitive NaCl-inducible RpoS-dependent channel (1,000 pS), YbiO (741 aas; 10TMSs).  Protects agains hypoosmotic shock (Edwards et al. 2012).


YbiO of E. coli (P75783)


Mechanosensitive channel, small conductance, YggB, GluE or MscCG (533 aas; 6-7 TMSs).  Mediates glutamate efflux (Becker et al. 2013).  The pore domain is in the N-terminus.  The C-terminus includes three subdomains, the periplasmic loop, the fourth transmembrane segment, and the cytoplasmic loop, all of which are important for MscCG function, in particular for glutamate excretion (Becker and Krämer 2015). Deletion of the encoding gene results in a 10% increase in lysine production and a decrease in cell mass yield (Xiao et al. 2020).



YggB or MscCG of Corynebacterium glutamicum (P42531)


MscCG2 of 334 aas and 4 TMSs in a 3 + 1 arrangement.  It functions as an L-glutamate exporter and an osmotic safety valve (Wang et al. 2018). It is 23% identical to MscCG (TC# 1.A.23.3.3) in the same organism. MscCG2-mediated L-glutamate excretion was activated by biotin limitation or penicillin treatment, and constitutive L-glutamate excretion was triggered by a gain-of-function mutation (A151V). It was not induced by glutamate producing conditions (Wang et al. 2018).

MscCG2 of Corynebacterium glutamicum


Small-conductance mechanosensitive channel Msc1 of 533 aas and 5 TMSs in a 4 (N-terminus) + 1 TMS (near the C-terminus) with two smaller peaks of hydrophobicity between these that could be TMSs. This system as well as a second Msc protein, Msc2, are able to export L-glutamate and other metabolites (Kawasaki and Martinac 2020).

Msc1 of Corynebacterium glutamicum


TC#NameOrganismal TypeExample
1.A.23.4.1The MscMJ mechanosensitive channelBacteria, archaea, yeast, plantsMscMJ of Methanococcus jannaschii

Uncharacterized MscS homologue


MscS homologue of Helicobacter pylori


Mitochondrial mechanosensitive ion channel protein 1, MscS-like channel, MSL1, of 497 aas and 5 TMSs. As the sole member of the Arabidopsis MSL family, localized in the mitochondrial inner membrane, MSL1 is essential for maintaining the normal membrane potential of mitochondria. Li et al. 2020 reported a cryoelectron microscopy (cryo-EM) structure of AtMSL1 at 3.3 Å. The overall architecture of AtMSL1 is similar to MscS, but the transmembrane domain of AtMSL1 is larger. Structural differences are observed in both the transmembrane and the matrix domain, and the carboxyl-terminus of AtMSL1 is more flexible while the beta-barrel structure observed in MscS is absent. The side portals in AtMSL1 are significantly smaller, and enlarging the size of the portal by mutagenesis can increase the channel conductance (Li et al. 2020).


MSL1 of Arabidopsis thaliana


Uncharacterized MscS channel of 351 aas and 4 N-terminal TMSs.

UP of Bdellovibrio bacteriovorus


MscS channel of 553 aas and 6 TMSs.

MscS of Entamoeba histolytica


Mechanosensitive channel-like 10, Msl10 of 734 aas and 5 or more TMSs.  It functions in triggering cell death in a process that is independent of its channel activity (Maksaev et al. 2018). The N-terminus of MSL10 (MSL10(N)) is an exemple of these IDRs. MSL10(N) adopted a predominately helical structure when exposed to the helix-inducing compound, trifluoroethanol (TFE), but in the presence of molecular crowding agents, MSL10(N) underwent structural changes and exhibited alterations to its homotypic interaction favorability. Collective behavior via in vitro imaging of condensates indicated that MSL8(N), MSL9(N), and MSL10(N) have sharply differing propensities for self-assembly into condensates, both inherently and in response to salt, temperature, and molecular crowding. These data establish the N-termini of MSL channels as IDRs with distinct biophysical properties and the potential to respond uniquely to changes in their physiochemical environments (Flynn et al. 2023).

Mscl10 of Arabidopsis thaliana (Mouse-ear cress)


Plasma membrane small conductance mechanosensitive channel, MSL4, of 881 aas and 5 putative TMSs (Hamilton et al. 2015). 

MSL4 of Arabidopsis thaliana


MscA, a mechanosensitive channel in the ER membranes of filamentous fungi (AN7571). It may have 6 or 7 TMSs in a 4 + 2 or 3 TMS arrangement, but there are also two moderately hydrophobic peaks near the C-terminus of the protein that might be TMSs. Orthologues of MscA and MscB are present in most fungi, including plant and animal pathogens. MscA/MscB and other fungal MscS-like proteins share the three TMSs and the extended C-terminal cytosolic domain that form the structural fingerprint of MscS-like channels (Dionysopoulou et al. 2022). Their overexpression leads to increased CaCl2 toxicity or/and reduction of asexual spore formation.

MscA of Emericella nidulans (Aspergillus nidulans)


MscB (AN6053) of 943 aas, a mechanosensitive channel in the PM membranes of filamentous fungi. It may have 6 or 7 TMSs in a 4 + 2 or 3 TMS arrangement, but there are also two moderately hydrophobic peaks near the C-terminus of the protein that might be TMSs. Orthologues of MscA and MscB are present in most fungi, including plant and animal pathogens. MscA/MscB and other fungal MscS-like proteins share the three TMSs and the extended C-terminal cytosolic domain that form the structural fingerprint of MscS-like channels (Dionysopoulou et al. 2022). Their overexpression leads to increased CaCl2 toxicity or/and reduction of asexual spore formation.

MscB of Emericella nidulans (Aspergillus nidulans)


Msy1 mechanosensitive calcium channel in response to hypo-osmotic shock. The protein is of 1011 aas with 6 or 7 TMSs in a 4 + 2 or 3 TMS arrangement. It regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock. The conductance is about 0.25 nanosiemens (Nakayama et al. 2012). It is involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypo-osmotic shock (Nakayama et al. 2014).

Msy1 of Schizosaccharomyces pombe (Fission yeast)




Msy2 of 840 aas and 7 or 8 TMSs in a 4 + 1 + 2 or 3 TMS arrangement. It regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock (Nakayama et al. 2012)., and is involved in maintaining vacuole integrity while protecting the nuclear envelope from hypo-osmotic shock (Nakayama et al. 2014).

Msy2 of Schizosaccharomyces pombe

1.A.23.4.2The MscMJLR mechanosensitive channelBacteria, archaea, yeast, plantsMscMJLR of Methanococcus jannaschii

Mechanosensitive ion channel protein, putative, of 1812 aas and 6 TMSs in a 4 (N-terminal) + 2 (central) TMS arrangement (Wunderlich, 2022).

MscS protein of Plasmodium falciparum



Mechanosensative cation-selective channel with a conductance of 100 pS, YnaI (344aas; 4 - 6 TMSs).  Protects against hypoosmotic shock (Edwards et al. 2012).  The structure has been solved by cryo-electron microscopy to a resolution of 13 Å (Böttcher et al. 2015). While the cytosolic vestibule is structurally similar to that in MscS, additional density is seen in the transmembrane region, consistent with the presence of two additional TMSs predicted for YnaI. The location of this density suggests that the extra TMSs are tilted, which could induce local membrane curvature extending the tension-sensing paddles seen in MscS. Off-center lipid-accessible cavities are seen that resemble gaps between the sensor paddles in MscS. The conservation of the tapered shape and the cavities in YnaI suggest a mechanism similar to that of MscS (Böttcher et al. 2015). The voltage dependence of inactivation occurs independently of the positive charges of R46, R54, and R74 (Nomura et al. 2016). A 3.8 Å structure by cryoEM revealed a heptamer structural fold similar to previously studied MscS channels. The ion-selective filter is formed by seven hydrophobic methionines (Met158) in the transmembrane pore (Yu et al. 2017). Details of the gating transition for MscS have been predicted (Zhu et al. 2018). YnaI has a gating mechanism based on flexible pore helices (Flegler et al. 2020), and thus, MscS-like channels of different sizes have a common core architecture but show different gating mechanisms and fine-tuned conductive properties. Attempted Cryo-EM structural determination of detergent-free YnaI Using SMA2000 revealed limitations of this method (Catalano et al. 2021).


YnaI of E. coli (P0AEB5)


Plant plastid mechanosensitive channel MscS-like-2 (Msl2) (controls plastid organellar morphology, as does Msl3) (Haswell and Meyerowitz, 2006Haswell et al., 2008). It functions as do the bacterial homologues, but is essential for leaf growth, chloroplast integrity and normal starch accumulation (Jensen and Haswell 2012).  msl2 msl3 double mutant seedlings exhibit several hallmarks of drought or environmental osmotic stress, including solute accumulation, elevated levels of the compatible osmolyte proline (Pro), and accumulation of the stress hormone abscisic acid (ABA). Furthermore, msl2 msl3 mutants expressed Pro and ABA metabolism genes in a pattern normally seen under drought or osmotic stress. Pro accumulation in the msl2 msl3 mutant was suppressed by conditions that reduce plastid osmotic stress leading to the conclusion that these channels function like their bacterial homologues (Wilson et al. 2014).


Msl2 of Arabidopsis thaliana (Q56X46)


MscM (YbdG) is a distant member of the MscS family. It displays miniconductance (MscM) activity (Schumann et al., 2010; Edwards et al. 2012).


MscM (YbdG) of E. coli (P0AAT4)


Mechanosensitive channel, MscS


MscS of Sulfolobus islandicus (C4KE93)


Mechanosensitive ion channel protein 8 (Mechanosensitive channel of small conductance-like 8) (MscS-like protein 8, Msl8) is a pollen-specific, membrane tension-gated ion channel required for pollen to survive the hypoosmotic shock of rehydration and for full male fertility. It negatively regulates pollen germination but is required for cellular integrity during germination and tube growth. MSL8 thus senses and responds to changes in membrane tension associated with pollen hydration and germination (Hamilton et al. 2015).  Mechanosensitive ion channels, MSL8, MSL9, and MSL10, have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics (Flynn et al. 2023).  Intrinsically disordered protein regions (IDRs) are highly dynamic sequences that rapidly sample a collection of conformations over time. In the past several decades, IDRs have emerged as major components of many proteomes, comprising ~30% of all eukaryotic protein sequences. Proteins with IDRs function in a wide range of biological pathways and are notably enriched in signaling cascades that respond to environmental stresses. Flynn et al. 2023 identified and characterized intrinsic disorder in the soluble cytoplasmic N-terminal domains of MSL8, MSL9, and MSL10, three members of the MscS-like (MSL) family of mechanosensitive ion channels. In plants, MSL channels are proposed to mediate cell and organelle osmotic homeostasis. See TC# 1.A.23.4.14 for details of MSL10.


MSL8 of Arabidopsis thaliana

1.A.23.4.8Mechanosensitive ion channel protein 5 (Mechanosensitive channel of small conductance-like 5) (MscS-Like protein 5)PlantsMSL5 of Arabidopsis thaliana

Putative small conductance mechanosensitive channel; Calcium channel, MacS


MacS of Mycosphaerella graminicola (Zymoseptoria tritici)


TC#NameOrganismal TypeExample

The cyclic nucleotide-binding MscS homologue, MT2508 (the C-terminal domain is the CAP_ED domain CD00038). It lacks mechanosensitivity but is ligand-gated by cyclic nucleotides (Caldwell et al., 2010).


MscS homologue, MT2508 of Mycobacterium tuberculosis (P71915)


TC#NameOrganismal TypeExample
1.A.23.6.1Chloroplast mechanosensitive channel, Msc1 (anions are preferred over cations) (Nakayama et al., 2007).


Msc1 of Chlamydomonas reinhardtii (A3KE12)


TC#NameOrganismal TypeExample

MscS homologue


MscS homologue of Streptomyces coelicolor


MscS homologue


MscS of Myxococcus xanthus


TC#NameOrganismal TypeExample

CmpX of 274 aas and 5 TMSs in a 1 + 4 arrangement. CmpX regulates virulence and controls biofilm formation in P. aeruginosa (Bhagirath et al. 2017). It also modulates intra-cellular c-di-GMP levels. A cmpX knockout showed decreased promoter activity of exoS (PA1362) and increased activity of the small RNA, RsmY. As compared to the wild-type PAO1, the cmpX mutant had elevated intracellular c-di-GMP levels as well as increased expression of wspR (PA3702), a c-di-GMP synthase. Transcription of the major outer membrane porin gene oprF (PA1777) and sigma factor sigX (PA1776) was decreased in the cmpX mutant. The cmpX knockout mutant had increased sensitivity to membrane detergents and antibiotics such as lauryl sulfobetaine, tobramycin, and vancomycin (Bhagirath et al. 2017). Exogenous c-di-GMP inhibits biofilm formation of Vibrio splendidus (Yang et al. 2023).

CmpX of Pseudomonas aeruginosa


CmpX protein of 227 aas and 5 TMSs

CmpX of Candidatus Wolfebacteria bacterium


Uncharacterized protein of 439 aas and 9 TMSs in a 5 + 4 arrangement.

UP of Brevundimonas viscosa


Mechanosensitive ion channel protein MscS of 254 aas and 5 TM

MscS of Haloterrigena daqingensis


Uncharacterized protein of 486 aas and 11 TMSs.

UP of Hydrogenophaga taeniospiralis