Difference between revisions of "SivA"
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Revision as of 14:51, 16 May 2013
- Description: inhibitor of KinA autophosphorylation, and subsequently of entry into sporulation
| Gene name | yweA |
| Synonyms | ipa-74d |
| Essential | no |
| Product | inhibitor of KinA autophosphorylation |
| Function | control of entry into sporulation via the phosphorelay |
| Gene expression levels in SubtiExpress: sivA | |
| MW, pI | 16 kDa, 7.175 |
| Gene length, protein length | 462 bp, 154 aa |
| Immediate neighbours | rocG, spsL |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU37800
Phenotypes of a mutant
- the sivA bslA double mutant exhibits a more severe loss of repellency of the biofilm surface as compared to the bslA mutant PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Protein family:
- Paralogous protein(s): BslA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane (according to Swiss-Prot)
- extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: P39632
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: sivA PubMed
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
Sharon Garti-Levi, Ashlee Eswara, Yoav Smith, Masaya Fujita, Sigal Ben-Yehuda
Novel modulators controlling entry into sporulation in Bacillus subtilis.
J Bacteriol: 2013, 195(7);1475-83
[PubMed:23335417]
[WorldCat.org]
[DOI]
(I p)
Kazuo Kobayashi, Megumi Iwano
BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms.
Mol Microbiol: 2012, 85(1);51-66
[PubMed:22571672]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818]
[WorldCat.org]
[DOI]
(P p)
