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Information on EC 2.7.1.211 - protein-Npi-phosphohistidine-sucrose phosphotransferase and Organism(s) Streptococcus mutans serotype c and UniProt Accession P12655

for references in articles please use BRENDA:EC2.7.1.211
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IUBMB Comments
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
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Streptococcus mutans serotype c
UNIPROT: P12655
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Word Map
The taxonomic range for the selected organisms is: Streptococcus mutans serotype C
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sucrose permease, enzyme iiscr, scrab, sucrose-specific enzyme ii, eiiscr, sucrose-specific transporter, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PTS system sucrose-specific EIIBCA component
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EIIScr
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Enzyme IIScr
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scrAB
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sucrose PTS permease
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:sucrose Npi-phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69983
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription regulator ScrR binds specifically to the promoter regions of both phosphotransferase gene ScrA and sucrose hydrolase gene ScrB. Mutations of high affinity regions OB and OC in the promoter sequences result in constitutive transcription and expression of both the ScrA and ScrB genes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, B.; Kuramitsu, H.K.
Control of enzyme IIscr and sucrose-6-phosphate hydrolase activities in Streptococcus mutans by transcriptional repressor ScrR binding to the cis-active determinants of the scr regulon
J. Bacteriol.
185
5791-5799
2003
Streptococcus mutans serotype c (P12655), Streptococcus mutans serotype c UA159 (P12655)
Manually annotated by BRENDA team
Sato, Y.; Poy, F.; Jacobson, G.R.; Kuramitsu, H.K.
Characterization and sequence analysis of the scrA gene encoding enzyme IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system
J. Bacteriol.
171
263-271
1989
Streptococcus mutans serotype c (P12655), Streptococcus mutans serotype c UA159 (P12655)
Manually annotated by BRENDA team
Zeng, L.; Burne, R.A.
Comprehensive mutational analysis of sucrose-metabolizing pathways in Streptococcus mutans reveals novel roles for the sucrose phosphotransferase system permease
J. Bacteriol.
195
833-843
2013
Streptococcus mutans serotype c (P12655), Streptococcus mutans serotype c UA159 (P12655)
Manually annotated by BRENDA team