Any feedback?
Information on EC 2.7.1.211 - protein-Npi-phosphohistidine-sucrose phosphotransferase
for references in articles please use BRENDA:EC2.7.1.211Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.211 protein-Npi-phosphohistidine-sucrose phosphotransferaseIUBMB 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.
Specify your search results
Word Map
- 2.7.1.211
-
phosphoenolpyruvate-dependent
- mutans
- sucrose-6-phosphate
-
symporter
- fructokinase
-
iiiglc
-
sucrose-metabolizing
-
antiterminates
- molasses
-
glucose-specific
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
sucrose permease, enzyme iiscr, scrab, sucrose-specific enzyme ii, eiiscr, sucrose-specific transporter, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cscB
EIIScr
Enzyme IIScr
PTS system sucrose-specific EIIBCA component
sacP
ScrA
scrAB
-
-
-
-
ScrR
sucrose permease
sucrose PTS permease
-
-
-
-
sucrose-specific enzyme II
sucrose-specific transporter
treB
trehalose(maltose)-specific PTS system components IIBC
EIIScr
-
-
-
-
Enzyme IIScr
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[protein]-Npi-phospho-L-histidine + sucrose[side 1] = [protein]-L-histidine + sucrose 6G-phosphate[side 2]
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6G-phosphate[side 2]
additional information
?
-
-
the reaction requires phosphoenolpyruvate, and 2-phosphoglycerate can only replace phosphoenolpyruvate in the absence of NaF
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6G-phosphate[side 2]
-
-
reaction product is sucrose phosphate
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6G-phosphate[side 2]
L06791
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6G-phosphate[side 2]
L06791
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + sucrose[side 1]
[protein]-L-histidine + sucrose 6'-phosphate[side 2]
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Rhinitis, Allergic
[Clinical characteristics of allergic rhinitis allergen spectrum in Gannan area].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is an regulatory protein EIII-independent protein in which the EII and EIII functional domains are covalently linked as a single polypeptide
L06791
GenBank
brenda
enzyme is an regulatory protein EIII-independent protein in which the EII and EIII functional domains are covalently linked as a single polypeptide
L06791
GenBank
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the protein has the hydropathic profile of an integral membrane protein lacking extended alpha-helical structures
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme is responsible for transporting the extracellular sucrose into the cell
metabolism
the enzyme is responsible for transporting the extracellular sucrose into the cell
physiological function
-
a mutant lacking sucrose phosphotransferase activity retains phosphotransferase activity for glucose, fructose, mannose, mannitol, sorbitol, lactose, and maltose
physiological function
deletion of repressor TreR enables uptake of sucrose via TreB, an enzyme II protein required for phoshotransferase mediated uptake of trehalose. Once inside the cell, this sucrose is not processed by the TreC hydrolase, nor is it sufficient for growth of the strain. Levels of cscA (invertase) transcript increase in the treR mutant relative to the wild-type strain when grown under low sucrose conditions
physiological function
-
distinct enzymes II for sucrose and glucose transport exist in Streptococcus mutans. Two integral membrane proteins, enzyme IIScr and enzyme IIG1c, each specific for its sugar substrate, sucrose or glucose, catalyze specific sugar:sugar-phosphate exchange reactions
physiological function
gene disruption does not result in a recognizable phenotype
physiological function
loss of phosphotransferase ScrA activity leads to growth stimulation on fructooligosaccharides, due in large part to increased expression of the fruAB (fructanase) operon. ScrA is required for activation of levD expression (a component of fructose/mannose-PTS EII permease) by sucrose through components of the LevQRST complex, but not for activation by the cognate LevQRST sugars fructose or mannose. Sucrose-dependent catabolite repression is also evident in strains containing an intact sucrose phosphotransferase system
physiological function
-
the sucrose permease lacks a sucrose-specific Enzyme III-like domain or a separate, soluble IIIScr protein. Enzyme IIScr is capable of utilizing the enzyme IIIGlc-like domain of the glucose permease. The IIIGlc-like domain therefore is an autonomous structural unit that assumes a conformation independent of the hydrophobic, N-terminal intramembranal domain of Enzyme IIGlc. Addition of the purified IIIGlc-like domain strongly stimulates the phosphorylation of sucrose, but not that of glucose, in phosphorylation assays that contain the two sugars simultaneously
physiological function
the sucrose phosphotransferase system of Streptococcus mutans is independent of regulatory enzyme III
physiological function
-
distinct enzymes II for sucrose and glucose transport exist in Streptococcus mutans. Two integral membrane proteins, enzyme IIScr and enzyme IIG1c, each specific for its sugar substrate, sucrose or glucose, catalyze specific sugar:sugar-phosphate exchange reactions
-
physiological function
-
deletion of repressor TreR enables uptake of sucrose via TreB, an enzyme II protein required for phoshotransferase mediated uptake of trehalose. Once inside the cell, this sucrose is not processed by the TreC hydrolase, nor is it sufficient for growth of the strain. Levels of cscA (invertase) transcript increase in the treR mutant relative to the wild-type strain when grown under low sucrose conditions
-
physiological function
-
the sucrose phosphotransferase system of Streptococcus mutans is independent of regulatory enzyme III
-
physiological function
-
loss of phosphotransferase ScrA activity leads to growth stimulation on fructooligosaccharides, due in large part to increased expression of the fruAB (fructanase) operon. ScrA is required for activation of levD expression (a component of fructose/mannose-PTS EII permease) by sucrose through components of the LevQRST complex, but not for activation by the cognate LevQRST sugars fructose or mannose. Sucrose-dependent catabolite repression is also evident in strains containing an intact sucrose phosphotransferase system
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1Y0Q4Y4_KLEPN
456
10
48022
TrEMBL
-
A0A8G1B9I6_STRSZ
627
10
65656
TrEMBL
-
A0A8F8Y8J3_LACPN
641
10
68391
TrEMBL
-
A0A812BXT1_SEPPH
208
3
24443
TrEMBL
other Location (Reliability: 5)
A0A653I8I2_9BACL
470
10
49644
TrEMBL
-
A0A0H3F7X9_ECOLW
Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W)
473
0
51130
TrEMBL
-
E0IXR1_ECOLW
Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W)
415
0
46926
TrEMBL
-
PTSBC_BACSU
Bacillus subtilis (strain 168)
461
0
49397
Swiss-Prot
Mitochondrion (Reliability: 4)
PTS3B_STRMU
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
664
0
69989
Swiss-Prot
other Location (Reliability: 4)
PTSBC_KLEPN
456
0
48022
Swiss-Prot
Chloroplast (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no signal peptide is found
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure. The sequence contains six putative transmembrane helices with three short periplasmic loops and three large intracellular domains
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus amyloliquefaciens 3DELTA strain
expression in Escherichia coli
expressed in Bacillus amyloliquefaciens 3DELTA strain
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
brenda
Steen, J.A.; Bohlke, N.; Vickers, C.E.; Nielsen, L.K.
The trehalose phosphotransferase system (PTS) in E. coli W can transport low levels of sucrose that are sufficient to facilitate induction of the csc sucrose catabolism operon
PLoS ONE
9
e88688
2014
Escherichia coli (A0A0H3F7X9), Escherichia coli DSM 1116 (A0A0H3F7X9)
brenda
Martin, E.; Wittenberger, C.
Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans
Infect. Immun.
24
865-868
1979
Streptococcus mutans
brenda
Jacobson, G.R.; Mimura, C.S.; Scott, P.J.; Thompson, P.W.
Identification and properties of distinct sucrose and glucose phosphotransferase enzyme II activities in Streptococcus mutans 6715g
Infect. Immun.
46
854-856
1984
Streptococcus mutans, Streptococcus mutans 6715g
brenda
Chen, Y.Y.; Lee, L.N.; LeBlanc, D.J.
Sequence analysis of scrA and scrB from Streptococcus sobrinus 6715
Infect. Immun.
61
2602-2610
1993
Streptococcus sobrinus (L06791), Streptococcus sobrinus, Streptococcus sobrinus 6715 (L06791), Streptococcus sobrinus 6715
brenda
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)
brenda
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)
brenda
Sutrina, S.L.; Reddy, P.; Saier, M.H.; Reizer, J.
The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease
J. Biol. Chem.
265
18581-18589
1990
Bacillus subtilis
brenda
Wagner, E.; Götz, F.; Brückner, R.
Cloning and characterization of the scrA gene encoding the sucrose-specific Enzyme II of the phosphotransferase system from Staphylococcus xylosus
Mol. Gen. Genet.
241
33-41
1993
Staphylococcus xylosus (P51184), Staphylococcus xylosus
brenda
Titgemeyer, F.; Jahreis, K.; Ebner, R.; Lengeler, J.W.
Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae and plasmid pUR400, which encode the sucrose transport protein Enzyme II Scr of the phosphotransferase system and a sucrose-6-phosphate invertase
Mol. Gen. Genet.
250
197-206
1996
Klebsiella pneumoniae (P27219), Klebsiella pneumoniae, Klebsiella pneumoniae KAY2026 (P27219)
brenda
Ebner, R.; Lengeler, J.
DNA sequence of the gene scrA encoding the sucrose transport protein EnzymeII(Scr) of the phosphotransferase system from enteric bacteria: homology of the EnzymeII(Scr) and EnzymeII(Bgl) proteins.
Mol. Microbiol.
2
9-17
1988
Salmonella enterica subsp. enterica serovar Typhimurium (P08470)
brenda
Morabbi Heravi, K.; Altenbuchner, J.
Cross talk among transporters of the phosphoenolpyruvate-dependent phosphotransferase system in Bacillus subtilis
J. Bacteriol.
200
e00213-18
2018
Bacillus subtilis (P05306), Bacillus subtilis 168 (P05306)
brenda
Feng, J.; Gu, Y.; Quan, Y.; Gao, W.; Dang, Y.; Cao, M.; Lu, X.; Wang, Y.; Song, C.; Wang, S.
Construction of energy-conserving sucrose utilization pathways for improving poly-gamma-glutamic acid production in Bacillus amyloliquefaciens
Microb. Cell Fact.
16
98
2017
Bifidobacterium animalis subsp. lactis, Escherichia coli (E0IXR1), Escherichia coli
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.1.211)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
Server: brenda1