PtsH
- 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: PtsH | |
MW, pI | 9,1 kDa, 4.58 |
Gene length, protein length | 264 bp, 88 amino acids |
Immediate neighbours | ptsG, ptsI |
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
phosphotransferase systems, transcription factors and their control, phosphoproteins, most abundant proteins
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
- BsubCyc: BSU13900
- 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:
- Effectors of protein activity:
- Interactions:
- HprK-HPr PubMed
- Enzyme I-HPr
- HPr-PtsG PubMed, PtsH-MtlF PubMed, ManP-HPr, GmuA-HPr
- GamP-HPr, BglP-HPr, LicA-HPr, LevD-HPr
- FruA-HPr, YpqE-HPr
- HPr-LicT, HPr-SacY, HPr-SacT, HPr-GlcT
- HPr-MtlR PubMed, HPr-LicR, HPr-LevR,HPr-ManR
- HPr-GlpK
- GapA-HPr PubMed
- HPr(Ser-46)-P-CcpA PubMed
- HPr-RbsR PubMed
- HPr(His)-P-RhgR PubMed
- Localization: cytoplasm PubMed
Database entries
- BsubCyc: BSU13900
- 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:
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 352 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 7193 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 914 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5795 PubMed
Biological materials
- Mutant: available in Jörg Stülke's lab:
- Expression vector:
- pGP438 (with N-terminal Strep-tag, in pGP172), available in Jörg Stülke's lab
- pAG2 (His-tag) PubMed, available in Anne Galinier lab
- pGP371(expression / purification of HPr-S46A, with His-tag from E. coli, in pWH844), available in Jörg Stülke's lab
- pGP1415 (HPr, expression in B. subtilis, from pBQ200), available in Jörg Stülke's lab
- pGP961 (HPr, expression in B. subtilis with N-terminal Strep-tag, for SPINE, available in Jörg Stülke's lab
- pGP1416 (HPr-H15A, expression in B. subtilis, from pBQ200), available in Jörg Stülke's 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 Jörg Stülke's lab
- Antibody: available in Jörg Stülke's 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