YsbA

• Description: putative anti-holin
  
  

Gene name	ysbA
Synonyms	lrgA
Essential	no
Product	putative anti-holin
Function	unknown
Gene expression levels in SubtiExpress: ysbA
MW, pI	15 kDa, 9.825
Gene length, protein length	438 bp, 146 aa
Immediate neighbours	ysbB, lytT
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

membrane proteins, proteins of unknown function

The gene

Basic information

• Locus tag: BSU28910

Phenotypes of a mutant

• • ysbAB mutant is delayed in pellicle formation (Chen et al)
  • ywbHG-yxaKC-ysbAB triple mutant is severely delayed in pellicle formation (Chen et al)

Database entries

• BsubCyc: BSU28910

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: LrgA subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cell membrane (according to Swiss-Prot)

Database entries

• BsubCyc: BSU28910

• Structure:

• UniProt: P94515

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: ysbA-ysbB PubMed

• Expression browser: ysbA PubMed

• Sigma factor:

• Regulation:
  • ysbAB expression is induced by acetate (Chen et al)

• Regulatory mechanism:

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
  • the expression of the ysbA-ysbB operon is strongly increased in a cshA mutant PubMed

Biological materials

• Mutant:
  • GP1554 (ysbA-ysbB::spc), available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Martin Lehnik-Habrink, Leonie Rempeters, Ákos T Kovács, Christoph Wrede, Claudia Baierlein, Heike Krebber, Oscar P Kuipers, Jörg Stülke
DEAD-Box RNA helicases in Bacillus subtilis have multiple functions and act independently from each other.
J Bacteriol: 2013, 195(3);534-44
[PubMed:23175651] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Kelly C Rice, Ethan E Mann, Jennifer L Endres, Elizabeth C Weiss, James E Cassat, Mark S Smeltzer, Kenneth W Bayles
The cidA murein hydrolase regulator contributes to DNA release and biofilm development in Staphylococcus aureus.
Proc Natl Acad Sci U S A: 2007, 104(19);8113-8
[PubMed:17452642] [WorldCat.org] [DOI] (P p)

Kelly C Rice, Jeremy B Nelson, Toni G Patton, Soo-Jin Yang, Kenneth W Bayles
Acetic acid induces expression of the Staphylococcus aureus cidABC and lrgAB murein hydrolase regulator operons.
J Bacteriol: 2005, 187(3);813-21
[PubMed:15659658] [WorldCat.org] [DOI] (P p)