Difference between revisions of "EpsA"
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* '''Mutant:''' | * '''Mutant:''' | ||
− | ** GP1517 (aphA3), available in [[ Jörg Stülke]]'s lab | + | ** GP1517 (aphA3) {{PubMed|24493247}}, available in [[ Jörg Stülke]]'s lab |
− | ** GP1519 (''[[epsA]]-[[epsB]]'', aphA3), available in [[ Jörg Stülke]]'s lab | + | ** GP1519 (''[[epsA]]-[[epsB]]'', aphA3) {{PubMed|24493247}}, available in [[ Jörg Stülke]]'s lab |
− | ** GP1567 ''[[epsA]]''::aphA3 ''[[tkmA]]''::spc, available in [[ Jörg Stülke]]'s lab | + | ** GP1567 ''[[epsA]]''::aphA3 ''[[tkmA]]''::spc {{PubMed|24493247}}, available in [[ Jörg Stülke]]'s lab |
* '''Expression vector:''' | * '''Expression vector:''' | ||
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* '''lacZ fusion:''' | * '''lacZ fusion:''' | ||
− | * '''GFP fusion:''' GP1569 epsA-gfp (spc) | + | * '''GFP fusion:''' GP1569 epsA-gfp (spc), available in [[ Jörg Stülke]]'s lab |
− | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[ Jörg Stülke]]'s lab | + | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]) {{PubMed|24493247}}, available in [[ Jörg Stülke]]'s lab |
* '''Antibody:''' | * '''Antibody:''' | ||
− | * '''FLAG-tag construct:''' GP1526 epsA-FLAG 3x spc (based on [[pGP1331]]) available in [[ Jörg Stülke]]'s lab | + | * '''FLAG-tag construct:''' GP1526 epsA-FLAG 3x spc (based on [[pGP1331]]) {{PubMed|24493247}}, available in [[ Jörg Stülke]]'s lab |
=Labs working on this gene/protein= | =Labs working on this gene/protein= |
Revision as of 12:54, 6 February 2014
- Description: extracellular polysaccharide synthesis, putative transmembrane modulator of EpsB activity, might activate EpsB autophosphorylation and substrate phosphorylation
Gene name | epsA |
Synonyms | yveK |
Essential | no |
Product | unknown |
Function | biofilm formation |
Gene expression levels in SubtiExpress: epsA | |
Interactions involving this protein in SubtInteract: EpsA | |
Regulation of this protein in SubtiPathways: epsA | |
MW, pI | 25 kDa, 6.071 |
Gene length, protein length | 702 bp, 234 aa |
Immediate neighbours | epsB, slrR |
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
protein modification, biofilm formation, membrane proteins
This gene is a member of the following regulons
AbrB regulon, RemA regulon, SinR regulon
The gene
Basic information
- Locus tag: BSU34370
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: cpsC/capA family (according to Swiss-Prot)
- Paralogous protein(s): TkmA
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P71050
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
- induction by sequestration of SinR by SinI or SlrA PubMed or by SlrR PubMed
- the epsA-epsB-epsC-epsD-epsE-epsF-epsG-epsH-epsI-epsJ-epsK-epsL-epsM-epsN-epsO operon is not expressed in a ymdB mutant PubMed
- the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed
Biological materials
- Mutant:
- GP1517 (aphA3) PubMed, available in Jörg Stülke's lab
- GP1519 (epsA-epsB, aphA3) PubMed, available in Jörg Stülke's lab
- GP1567 epsA::aphA3 tkmA::spc PubMed, available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion: GP1569 epsA-gfp (spc), available in Jörg Stülke's lab
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH) PubMed, available in Jörg Stülke's lab
- Antibody:
- FLAG-tag construct: GP1526 epsA-FLAG 3x spc (based on pGP1331) PubMed, available in Jörg Stülke's lab
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
Reviews
Original publications