HPr, General component of the sugar [SW|phosphotransferase system] (PTS)
function
PTS-dependent sugar transport and carbon catabolite repression
product
histidine-containing phosphocarrier protein HPr of the PTS
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.2|Transporters] → [category|SW 1.2.2|Phosphotransferase system] → [category|SW 1.2.2.1|General PTS proteins][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.2|Transcription factors and their control] → [category|SW 3.4.2.7|Control of transcription factor (other than two-component system)][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.4|Phosphorylation on a His residue][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.5|Phosphorylation on a Ser residue]Gene
Coordinates
1,459,384 1,459,650
The protein
Protein family
HPr family (with [protein|A269774F2FDC94F93BA5F1360FFFE754B50383AD|Crh], according to UniProt)Paralogous protein(s)
[protein|A269774F2FDC94F93BA5F1360FFFE754B50383AD|Crh] [SW|Domains]
HPr domain (aa 2-88) (according to UniProt)Modification
transient phosphorylation by [protein|14ED1AF5038F43F3B151FCBABE6CFC5A2DA3AA6E|Enzyme I] of the PTS on His-15regulatory phosphorylation on Ser-46 by [protein|771F205F818A755A661B8E1C95365A4F6AEB05C7|HprK] [Pubmed|2507315]an extensive study on ''in vivo'' HPr phosphorylation can be found in Singh et al. (2008) [PubMed|18757537]weak phosphorylation on Ser-12 [Pubmed|17218307]''in vitro'' phosphorylated by [protein|23FF4A00C36EC1B7297F51A9EF3579B41F0B7EBA|PrkC] on Ser-12 [Pubmed|20389117]Structure
[PDB|2HID] (NMR) [Pubmed|9336834][PDB|1KKM] (complex of ''L. casei'' [protein|771F205F818A755A661B8E1C95365A4F6AEB05C7|HprK] with ''B. subtilis'' HPr-Ser-P)[PDB|1KKL] (complex of ''Lactobacillus casei'' [protein|771F205F818A755A661B8E1C95365A4F6AEB05C7|HprK] with ''B. subtilis'' HPr)[PDB|3OQM] (complex of ''B. subtilis'' [protein|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA] with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and the [gene|DAA285C86692E8B47D48652E0973AE3FF091CBC3|ackA] operator site)[PDB|3OQN] (complex of ''B. subtilis'' [protein|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA] with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and the [gene|1C566E54F8EF1A17A365FC49DFDA452AC5D0CA64|gntR] operator site)[PDB|3OQO] (complex of ''B. subtilis'' [protein|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA] with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and a optimal synthetic operator site)[SW|Localization]
cytoplasm [Pubmed|23475962]additional information
belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Expression and Regulation
Operons
genes
[gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]-[gene|14ED1AF5038F43F3B151FCBABE6CFC5A2DA3AA6E|ptsI]
description
[Pubmed|11902727]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|11902727], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]view in new tabgenes
[gene|B5E7EB475434E96786C577AE709A21BD702733D8|ptsG]-[gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]-[gene|14ED1AF5038F43F3B151FCBABE6CFC5A2DA3AA6E|ptsI]
description
[Pubmed|11902727]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|11902727], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]regulatory mechanism
[regulon|stringent response|stringent response]: negative regulation, in [regulon|stringent response|stringent response][protein|BC0DF593AE969F1DBC5E9E2BACF1C00BE4FEE449|GlcT]: antitermination, via the [protein|BC0DF593AE969F1DBC5E9E2BACF1C00BE4FEE449|GlcT]-dependent [SW|RNA switch] [PubMed|9765562], in [regulon|BC0DF593AE969F1DBC5E9E2BACF1C00BE4FEE449|GlcT regulon]regulation
expression activated by glucose (2 fold) ([protein|search|GlcT]) [Pubmed|12850135]view in new tabBiological materials
Mutant
available in [SW|Jörg Stülke]'s lab:MZ303 (cat)GP507 [gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]1 (S46A)GP506 ([gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]-H15A)GP778 (Δ[gene|BC0DF593AE969F1DBC5E9E2BACF1C00BE4FEE449|glcT]-[gene|B5E7EB475434E96786C577AE709A21BD702733D8|ptsG]-[gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]-[gene|14ED1AF5038F43F3B151FCBABE6CFC5A2DA3AA6E|ptsI]::spc) [Pubmed|22722928]BKE13900 (Δ[gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]::erm trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKE13900 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAAGAATTGACCTCCTCT, downstream forward: _UP4_TAAGGGTGTTAGTACGCCGTBKK13900 (Δ[gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]::kan trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKK13900 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAAGAATTGACCTCCTCT, downstream forward: _UP4_TAAGGGTGTTAGTACGCCGTGFP fusion
GP1267, [gene|29B793660E4D30C0656248F3EF403FEF76FB9025|ptsH]-cfp, available in [SW|Jörg Stülke]'s lab [pubmed|23475962]Expression vectors
pGP438 (with N-terminal Strep-tag, in [SW|pGP172]), available in [SW|Jörg Stülke]'s labpAG2 (His-tag) [Pubmed|9237995], available in [SW|Anne Galinier] labpGP371(expression / purification of HPr-S46A, with His-tag from ''E. coli'', in [SW|pWH844]), available in [SW|Jörg Stülke]'s labpGP1415 (HPr, expression in ''B. subtilis'', from [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP961 (HPr, expression in ''B. subtilis'' with N-terminal Strep-tag, for [SW|SPINE], available in [SW|Jörg Stülke]'s labpGP1416 (HPr-H15A, expression in ''B. subtilis'', from [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP2431 (N-terminal Strep-tag, expression and purification from ''B. subtilis'', in [SW|pGP380]), for [SW|SPINE], available in [SW|Jörg Stülke]'s labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labAntibody
available in [SW|Jörg Stülke]'s lablabs
[SW|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage][SW|Richard Brennan], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage][SW|Boris Görke], Max Perutz Center, Vienna, Austria[SW|Anne Galinier], University of Marseille, FranceReferences
16519689,12850135,17218307,16519689,17142398,12359875,1577686,9162046,11929549,9336834,7803390,7623661,2846556,8169206,9973552,15126459,10048041,12169607,9622354,10217795,17693724,18757537,9202047,7592487,15369672,14527945,2507315,8580838,19651770,8418852,26282429,1303754,1549615,20081037,20389117,20444094,22001508,22722928,23551403,15378759,26381121,9336834,23475962