rasP

rasP
168

intramembrane protease, cleaves FtsL, RsiV, RsgI and RsiW as well as signal peptides after release of the secreted proteins

Locus
BSU_16560
Molecular weight
46.58 kDa
Isoelectric point
5.14
Protein length
Gene length
Function
control of cell division, and SigV and SigW activity
Product
intramembrane protease
Essential
no
Synonyms
rasP, yluC

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0750 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,724,029 → 1,725,297
Phenotypes of a mutant
defects in competence development, protein secretion and membrane protein production PubMed
mutants grow slower in liquid, are not competent, can’t activate SigW, have cell division defects, and decreased long term survival PubMed
inactivation of rasP reduces sporulation efficiency to 1.4% that of wild type cells; delayed entry into sporulation; thin, oblong forespores PubMed
a cwlO rasP mutant is not viable, due to lack of expression of lytE PubMed
ponA rasP double mutants have a growth defect that can be suppressed by reduced fatty acid synthesis (mutations in accA, accB, accC, accD or downregulation of the FapR regulon due to specific mutations in fapR) PubMed
The protein
Catalyzed reaction/ biological activity
cleaves FtsL, RsiV and RsiW
cleaves signal peptides after release  of the secreted proteins PubMed
Protein family
peptidase M50B family (according to UniProt)
4 transmembrane helices (aa 6 - 26, 175 - 195, 346 - 366, 394 - 414) (according to UniProt)
PDZ domain (aa 190 - 268) (according to UniProt)
Structure
cell membrane PubMed
Expression and Regulation
Operons
Description
Open in new tab

ispCpolC

2025-07-15 02:52:09

Jstuelk

200

babdb9046d2f2d5bae4dac8092e2f7235f01c3e9

23B0B9EE13D6BD9F4D99911E7AA88933F4080154

Description
Open in new tab

uppSpolC

2025-07-13 15:39:04

Jstuelk

153

c6a20b58d42a343484ae9ff8f9312018bf0f82f2

3AF78B34597AE93B1AF63769A0A2561D91069003

Additional information
expression is reduced in motile cells as compared to non-motile cells PubMed
Biological materials
Mutant
BKE16560 (ΔrasP::erm  trpC2) available at BGSCPubMed, upstream reverse: _UP1_AACTGTATTCACGAACATAC,  downstream forward: _UP4_TAAACGAAAAGTAAATCAAT
BKK16560 (ΔrasP::kan  trpC2) available at BGSCPubMed, upstream reverse: _UP1_AACTGTATTCACGAACATAC,  downstream forward: _UP4_TAAACGAAAAGTAAATCAAT
References
Reviews
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Original Publications
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CB50289535EA537F63BADD459BD11AA7759A6658

Page visits: 5853

Time of last update: 2025-07-14 17:08:58

Author of last update: Jstuelk