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

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

Database entries

• DBTBS entry: [1]

• SubtiList entry:[2]

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:
  • transient phosphorylation by Enzyme I of the PTS on His-15
  • regulatory phosphorylation on Ser-46 by HprK PubMed
  • an extensive study on in vivo HPr phosphorylation can be found in Singh et al. (2008) PubMed
  • weak phosphorylation on Ser-12 PubMed
  • in vitro phosphorylated by PrkC on Ser-12 PubMed

• Cofactor(s):

• 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-YesS PubMed

• Localization: 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.-

Expression and regulation

• Operon:
  • ptsG-ptsH-ptsI PubMed
  • ptsH-ptsI PubMed

• Expression browser: ptsH PubMed

• Sigma factor:
  • ptsG: SigA PubMed
  • ptsH: SigA PubMed

• Regulation:
  • expression activated by glucose (2 fold) (GlcT) PubMed
  • the ptsH promoter is constitutive PubMed
  • subject to negative stringent control upon amino acid limitation (due to control of ptsG transcription initiation) PubMed

• Regulatory mechanism:
  • ptsG: transcriptional antitermination via the GlcT-dependent RNA switch PubMed

• Additional information:

Biological materials

• Mutant: available in Jörg Stülke's lab:
  • MZ303 (cat)
  • GP507 ptsH1 (S46A)
  • GP506 (ptsH-H15A)
  • GP777 (replacement of glcT and the ptsG-ptsH-ptsI operon by a spc cassette), PubMed

• 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