ptsG

ptsG
168

glucose permease of the phosphotransferase system, EIICBA of the PTS, Trigger enzyme, control of GlcT activity

Locus
BSU_13890
Molecular weight
75.34 kDa
Isoelectric point
5.41
Protein length
Gene length
Function
glucose transport and phosphorylation, control of GlcT activity
Product
glucose permease, trigger enzyme
Essential
no
E.C.
2.7.1.69
Synonyms
ptsG, ptsX, crr

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG2190 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,457,187 → 1,459,286
The protein
Catalyzed reaction/ biological activity
transport and phosphorylation of glucose, receives a phosphate from HPr]] at the IIA domain (His-620), the phosphate group is then transferred to the IIB domain (Cys-461) an finally to the incoming glucose. In the absence of glucose, PtsG phosphorylates and thereby inactivates the transcriptional antiterminator GlcT.
D-glucose + Nπ-phospho-L-histidyl-[protein] --> D-glucose-6-P + L-histidyl-[protein] (according to UniProt)
Protein family
PTS permease, glucose family PubMed
11x transmembrane domain (16–36, 89–109, 139–159, 180–200, 233–253, 283–303, 313–333, 338–358, 365–385, 388–408)
PTS EIIA domain type-1 (aa 568–672) (according to UniProt)
PTS EIIB domain type-1 (aa 439–520) (according to UniProt)
PTS EIIC domain type-1 (aa 1-424) (according to UniProt)
Structure
8QSR (PDB) (the IIC dimer of E. coli PtsG, 47% identity) PubMed
5IWS (PDB) (the IIC domain of B. cereus MalT, 32% identity) PubMed
1AX3 (PDB) (IIA domain) PubMed
1GPR (PDB) (IIA domain)
Modification
transient  phosphorylation (HPr]]-dependent) on His-620, then internal phosphotransfer from His-620 to Cys-461
Paralogous protein(s)
membrane protein PubMed
Expression and Regulation
Operons
Description
Regulation
expression activated by glucose (2 fold) (GlcT) PubMed
Regulatory mechanism
stringent response: negative regulation, in stringent response
GlcT: antitermination, via the GlcT-dependent RNA switch PubMed, in glcT regulon
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
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ptsGptsI

2025-01-14 22:20:32

ghost

149

0d1ff574eb4a847a56452c8c7084e1e199118b30

EEB2B4E2EFD5EB6876956633E22D1305FFE807F7

Biological materials
Mutant
GP778 (ΔglcT-ptsG-ptsH-ptsI::spc) PubMed, available in Jörg Stülke's lab
BKE13890 (ΔptsG::erm  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATAAGAATTGACCTCCTCT,  downstream forward: _UP4_TAAGGGTGTTAGTACGCCGT
BKK13890 (ΔptsG::kan  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATAAGAATTGACCTCCTCT,  downstream forward: _UP4_TAAGGGTGTTAGTACGCCGT
Expression vectors
pGP123 (domains BA, in pWH844), available in Jörg Stülke's lab
pGP141 (domains BA, mut: H620D, in pWH844), available in Jörg Stülke's lab
pGP428 (EIIB, in pWH844), available in Jörg Stülke's lab
pGP437(EIIA in pGP570, with thrombin cleavage site), available in Jörg Stülke's lab
LacZ fusion
pGP34 (pAC5) PubMed, available in Jörg Stülke's lab
pGP66 (pAC7) PubMed, available in Jörg Stülke's lab
pGP606 (mutant terminator, pAC6), available in Jörg Stülke's lab
pGP532 (pAC7), available in Jörg Stülke's lab
series of promoter deletions are available in pAC5 and pAC6, available in Jörg Stülke's lab
series of RAT mutants are available in pAC6, available in Jörg Stülke's lab
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
References
Reviews
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Original Publications
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Page visits: 9474

Time of last update: 2025-01-24 19:52:57

Author of last update: Jstuelk