Difference between revisions of "SpoIVFB"
Line 52: | Line 52: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' processing of pro-sigma-K to active [[SigK]] | + | * '''Catalyzed reaction/ biological activity:''' processing of pro-sigma-K to active [[SigK]] {{PubMed|19805276}} |
* '''Protein family:''' peptidase M50B family (according to Swiss-Prot) | * '''Protein family:''' peptidase M50B family (according to Swiss-Prot) | ||
Line 63: | Line 63: | ||
* '''Domains:''' | * '''Domains:''' | ||
+ | ** C-terminal cystathionine-beta-synthase (CBS) domain, this domain binds ATP {{PubMed|19805276}} | ||
* '''Modification:''' | * '''Modification:''' | ||
Line 68: | Line 69: | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
− | * '''Effectors of protein activity:''' | + | * '''Effectors of protein activity:''' ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level {{PubMed|19805276}} |
− | * '''Interactions:''' [[SpoIVFB]]-pro[[SigK]] | + | * '''Interactions:''' [[SpoIVFB]]-pro[[SigK]] {{PubMed|19805276}} |
* '''Localization:''' cell membrane | * '''Localization:''' cell membrane | ||
Line 118: | Line 119: | ||
=References= | =References= | ||
− | <pubmed>11959848,9501233,12940997,1577688,12060714,9078383,1942049,10611287, 16818230 </pubmed> | + | <pubmed>11959848,9501233,12940997,1577688,12060714,9078383,1942049,10611287, 16818230 19805276 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:54, 8 October 2009
- Description: intramembrane metalloprotease, processing of pro-sigma-K to active SigK
Gene name | spoIVFB |
Synonyms | |
Essential | no |
Product | intramembrane metalloprotease |
Function | processing of pro-sigma-K to active SigK |
MW, pI | 33 kDa, 8.483 |
Gene length, protein length | 864 bp, 288 aa |
Immediate neighbours | rplU, spoIVFA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU27970
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Protein family: peptidase M50B family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- C-terminal cystathionine-beta-synthase (CBS) domain, this domain binds ATP PubMed
- Modification:
- Cofactor(s):
- Effectors of protein activity: ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level PubMed
- Localization: cell membrane
Database entries
- Structure:
- UniProt: P26937
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- 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
Ruanbao Zhou, Christina Cusumano, Dexin Sui, R Michael Garavito, Lee Kroos
Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.
Proc Natl Acad Sci U S A: 2009, 106(38);16174-9
[PubMed:19805276]
[WorldCat.org]
[DOI]
(I p)
Nathalie Campo, David Z Rudner
A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis.
Mol Cell: 2006, 23(1);25-35
[PubMed:16818230]
[WorldCat.org]
[DOI]
(P p)
Tran C Dong, Simon M Cutting
SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro-sigmaK in Bacillus subtilis.
Mol Microbiol: 2003, 49(5);1425-34
[PubMed:12940997]
[WorldCat.org]
[DOI]
(P p)
David Z Rudner, Qi Pan, Richard M Losick
Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture.
Proc Natl Acad Sci U S A: 2002, 99(13);8701-6
[PubMed:12060714]
[WorldCat.org]
[DOI]
(P p)
David Z Rudner, Richard Losick
A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization.
Genes Dev: 2002, 16(8);1007-18
[PubMed:11959848]
[WorldCat.org]
[DOI]
(P p)
D Z Rudner, P Fawcett, R Losick
A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors.
Proc Natl Acad Sci U S A: 1999, 96(26);14765-70
[PubMed:10611287]
[WorldCat.org]
[DOI]
(P p)
O Resnekov, R Losick
Negative regulation of the proteolytic activation of a developmental transcription factor in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1998, 95(6);3162-7
[PubMed:9501233]
[WorldCat.org]
[DOI]
(P p)
O Resnekov, S Alper, R Losick
Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis.
Genes Cells: 1996, 1(6);529-42
[PubMed:9078383]
[WorldCat.org]
[DOI]
(P p)
E Ricca, S Cutting, R Losick
Characterization of bofA, a gene involved in intercompartmental regulation of pro-sigma K processing during sporulation in Bacillus subtilis.
J Bacteriol: 1992, 174(10);3177-84
[PubMed:1577688]
[WorldCat.org]
[DOI]
(P p)
S Cutting, S Roels, R Losick
Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis.
J Mol Biol: 1991, 221(4);1237-56
[PubMed:1942049]
[WorldCat.org]
[DOI]
(P p)