Subsystem: EcsAB transporter affecting expression and secretion of secretory preproteins

This subsystem's description is:

EcsAB transporter, present in Bacillus and many other Gram(+) microorganisms, has been grouped in a subfamily of extruders related to antibiotic-resistance systems, with similarities to possible efflux pumps for peptide antibiotics (Quentin et al., 1999). The actual substrate for EcsAB and its function is unknown, but it was hypothesized (Heinrich et al., 2008) that it transports peptides, possibly peptides that insert into the cytoplasmic membrane. It has been also suggested, that EscAB performs dual signal transduction functions affecting expression of secreted proteins as well as their secretion (Leslkela et al., 1999). Mutations in EcsA and EcsB cause a pleiotropic phenotype, including defects in competence development, sporulation and in formation biofilms. The most interesting phenotype of an EcsA-negative mutant is its inability to properly secrete alpha-amylase AmyQ. The preAmyQ precursor protein remains cell-associated but is accessible to tryptic digestion in protoplasts, pointing to a defect in its processing by signal peptidases.
Lack of EcsC function is not essential for the function of Ecs.

References

Heinrich J, Lundén T, Kontinen VP, Wiegert T. The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP.

Hyyryläinen HL, Sarvas M, Kontinen VP. Transcriptome analysis of the secretion stress response of Bacillus subtilis. Appl Microbiol Biotechnol. 2005 May;67(3):389-96. Epub 2005 Jan 27. PMID: 15856219

Leskelä S, Kontinen VP, Sarvas M. Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence. Microbiology. 1996 Jan;142 ( Pt 1):71-7. PMID: 8581172

Lulko AT, Veening JW, Buist G, Smits WK, Blom EJ, Beekman AC, Bron S, Kuipers OP. Production and secretion stress caused by overexpression of heterologous alpha-amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis. Appl Environ Microbiol. 2007 Aug;73(16):5354-62. Epub 2007 Jun 22. PMID: 17586671 [PubMed - indexed for MEDLINE] Related articlesFree article
Microbiology. 2008 Jul;154(Pt 7):1989-97. PMID: 18599827

Palva A, Sarvas M, Kontinen VP. Ecs, an ABC transporter of Bacillus subtilis: dual signal transduction functions affecting expression of secreted proteins as well as their secretion. Leskelä S, Wahlström E, Hyyryläinen HL, Jacobs M,. Mol Microbiol. 1999 Jan;31(2):533-43. PMID: 10027970

Pummi T, Leskelä S, Wahlström E, Gerth U, Tjalsma H, Hecker M, Sarvas M, Kontinen VP. ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter. J Bacteriol. 2002 Feb;184(4):1010-8. PMID: 11807061

For more information, please check out the description and the additional notes tabs, below

DiagramFunctional RolesSubsystem SpreadsheetDescriptionAdditional Notes 

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EcsAEscBEcsCFold*HypHpr
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EcsAB transporter, present in Bacillus and many other Gram(+) microorganisms, has been grouped in a subfamily of extruders related to antibiotic-resistance systems, with similarities to possible efflux pumps for peptide antibiotics (Quentin et al., 1999). The actual substrate for EcsAB and its function is unknown, but it was hypothesized (Heinrich et al., 2008) that it transports peptides, possibly peptides that insert into the cytoplasmic membrane. It has been also suggested, that EscAB performs dual signal transduction functions affecting expression of secreted proteins as well as their secretion (Leslkela et al., 1999). Mutations in EcsA and EcsB cause a pleiotropic phenotype, including defects in competence development, sporulation and in formation biofilms. The most interesting phenotype of an EcsA-negative mutant is its inability to properly secrete alpha-amylase AmyQ. The preAmyQ precursor protein remains cell-associated but is accessible to tryptic digestion in protoplasts, pointing to a defect in its processing by signal peptidases.
Lack of EcsC function is not essential for the function of Ecs.

References

Heinrich J, Lundén T, Kontinen VP, Wiegert T. The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP.

Hyyryläinen HL, Sarvas M, Kontinen VP. Transcriptome analysis of the secretion stress response of Bacillus subtilis. Appl Microbiol Biotechnol. 2005 May;67(3):389-96. Epub 2005 Jan 27. PMID: 15856219

Leskelä S, Kontinen VP, Sarvas M. Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence. Microbiology. 1996 Jan;142 ( Pt 1):71-7. PMID: 8581172

Lulko AT, Veening JW, Buist G, Smits WK, Blom EJ, Beekman AC, Bron S, Kuipers OP. Production and secretion stress caused by overexpression of heterologous alpha-amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis. Appl Environ Microbiol. 2007 Aug;73(16):5354-62. Epub 2007 Jun 22. PMID: 17586671 [PubMed - indexed for MEDLINE] Related articlesFree article
Microbiology. 2008 Jul;154(Pt 7):1989-97. PMID: 18599827

Palva A, Sarvas M, Kontinen VP. Ecs, an ABC transporter of Bacillus subtilis: dual signal transduction functions affecting expression of secreted proteins as well as their secretion. Leskelä S, Wahlström E, Hyyryläinen HL, Jacobs M,. Mol Microbiol. 1999 Jan;31(2):533-43. PMID: 10027970

Pummi T, Leskelä S, Wahlström E, Gerth U, Tjalsma H, Hecker M, Sarvas M, Kontinen VP. ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter. J Bacteriol. 2002 Feb;184(4):1010-8. PMID: 11807061
This SS can be used to analyze phyletic distribution of two subfamilies of histidine triad (HIT) proteins as part of the UofF Plan/Prokaryotic research project, namely:

(i) Putative histidine triad (HIT) protein, At5g48545 homolog
(ii) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) (EC 3.6.1.17)

These proteins often appear to colocalize with the escAB(C) genes