Difference between revisions of "PtsH"
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* '''GFP fusion:''' | * '''GFP fusion:''' | ||
+ | |||
+ | * '''CFP fusion:''' B. subtilis GP1267 ptsH-cfp ermC- without terminator, available in [[Jörg Stülke]]'s lab | ||
* '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Boris Görke| Görke]] lab | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Boris Görke| Görke]] lab |
Revision as of 11:52, 1 October 2012
- Description: HPr, General component of the sugar phosphotransferase system (PTS).
Gene name | ptsH |
Synonyms | |
Essential | no |
Product | histidine-containing phosphocarrier protein HPr of the PTS |
Function | PTS-dependent sugar transport and carbon catabolite repression |
Gene expression levels in SubtiExpress: ptsH | |
Interactions involving this protein in SubtInteract: PtsH | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Sugar catabolism | |
MW, pI | 9,1 kDa, 4.58 |
Gene length, protein length | 264 bp, 88 amino acids |
Immediate neighbours | ptsG, ptsI |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
phosphotransferase systems, transcription factors and their control, phosphoproteins
This gene is a member of the following regulons
GlcT regulon, stringent response
The gene
Basic information
- Locus tag: BSU13900
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry:[2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine (according to Swiss-Prot) Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine
- Protein family: HPr domain (according to Swiss-Prot) HPr family
- Paralogous protein(s): Crh
Extended information on the protein
- Kinetic information:
- Domains: HPr Domain (2–88)
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot), Cytoplasm PubMed
Database entries
- Structure:
- 1KKM (complex of L. casei HprK with B. subtilis HPr-Ser-P)
- 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr)
- 2HID (NMR)
- 3OQM (complex of B. subtilis CcpA with P-Ser-HPr and the ackA operator site)
- 3OQN (complex of B. subtilis CcpA with P-Ser-HPr and the gntR operator site)
- 3OQO (complex of B. subtilis CcpA with P-Ser-HPr and a optimal synthetic operator site)
- UniProt: P08877
- KEGG entry: [3]
- E.C. number: 2.7.11.-
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- ptsG: transcriptional antitermination via the GlcT-dependent RNA switch PubMed
- Additional information:
Biological materials
- Mutant: available in Stülke lab
- Expression vector:
- pGP438 (with N-terminal Strep-tag, in pGP172), available in Stülke lab
- pAG2 (His-tag), available in Anne Galinier lab
- pGP371(expression / purification of HPr-S46A, with His-tag from E. coli, in pWH844), available in Stülke lab
- pGP1415 (HPr, expression in B. subtilis, from pBQ200), available in Stülke lab
- pGP961 (HPr, expression in B. subtilis with N-terminal Strep-tag, for SPINE, available in Stülke lab
- pGP1416 (HPr-H15A, expression in B. subtilis, from pBQ200), available in Stülke lab
- lacZ fusion:
- GFP fusion:
- CFP fusion: B. subtilis GP1267 ptsH-cfp ermC- without terminator, available in Jörg Stülke's lab
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab
- Antibody: available in Stülke lab
Labs working on this gene/protein
Josef Deutscher, Paris-Grignon, France
Jörg Stülke, University of Göttingen, Germany Homepage
Wolfgang Hillen, Erlangen University, Germany Homepage
Richard Brennan, Houston, Texas, USA Homepage
Boris Görke, University of Göttingen, Germany Homepage
Anne Galinier, University of Marseille, France
Your additional remarks
References