Literature summary for 2.7.3.9 extracted from

Mizrachi Nebenzahl, Y.; Blau, K.; Kushnir, T.; Shagan, M.; Portnoi, M.; Cohen, A.; Azriel, S.; Malka, I.; Adawi, A.; Kafka, D.; Dotan, S.; Guterman, G.; Troib, S.; Fishilevich, T.; Gershoni, J.M.; Braiman, A.; Mitchell, A.M.; Mitchell, T.J.; Porat, N.; Goliand, I.; Chalifa Caspi, V.; Swiatlo, E.; Tal, M.; Ellis, R.; Elia, N.; Dagan, R.
Streptococcus pneumoniae cell-wall-localized phosphoenolpyruvate protein phosphotransferase can function as an adhesin: identification of its host target molecules and evaluation of its potential as a vaccine (2016), PLoS ONE, 11, e0150320.

Application

Application	Comment	Organism
medicine	the enzyme can function as an adhesin, evaluation of its potential as a vaccine. Immunization with rPtsA protects mice against a sublethal intranasal and a lethal intravenous pneumococcal challenge. PtsA binding peptides derived from its putative target molecules can be considered for development of therapeutics, and rPtsA is a candidate for vaccine development	Streptococcus pneumoniae

Cloned (Comment)	Organism
gene ptsI, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, recombinant expression in Escherichia coli strain BL21(DE3)pLysS	Streptococcus pneumoniae

Inhibitors	Comment	Organism	Structure
additional information	enzyme PtsA binding peptides derived from its putative target molecules, i.e. AVVVNDANRTRK, ADDESPEMKPGX, TXQVSNHKNHTN, LDSIRIIVIRRI, ADGGVPV, and DQRPAXRRMYRA, inhibit pneumococcal adhesion in vitro to lung- and tracheal-derived cell lines. In addition, the tested peptides inhibit lung colonization after intranasal inoculation of mice with Streptococcus pneumoniae	Streptococcus pneumoniae

Localization	Comment	Organism	GeneOntology No.	Textmining
cell wall	-	Streptococcus pneumoniae	5618	-

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120100	-	recombinant untagged enzyme, mass spectrometry	Streptococcus pneumoniae

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Streptococcus pneumoniae	the enzyme can function as an adhesin, identification of host target molecules, overview	?	-	?
phosphoenolpyruvate + protein histidine	Streptococcus pneumoniae	-	pyruvate + protein Npi-phospho-L-histidine	-	?

Organism	UniProt	Comment	Textmining
Streptococcus pneumoniae	A0A0H2ZMY1	serotype 2 strain D39 and strain WU2, and the unencapsulated derivative of strain WU2, namely strain 3.8DW, and the unencapsulated derivative of strain D39, namely strain R6, gene ptsI	-

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme can function as an adhesin, identification of host target molecules, overview	Streptococcus pneumoniae	?	-	?
phosphoenolpyruvate + protein histidine	-	Streptococcus pneumoniae	pyruvate + protein Npi-phospho-L-histidine	-	?

Subunits	Comment	Organism
dimer	2 * 63165,sequence calculation, 2 * 70000-72000, recombinant untagged enzyme, SDS-PAGE, 2 * 62492-63932, recombinant untagged enzyme, mass spectrometry	Streptococcus pneumoniae

Synonyms	Comment	Organism
phosphoenolpyruvate protein phosphotransferase	-	Streptococcus pneumoniae
ptsA	-	Streptococcus pneumoniae

General Information	Comment	Organism
physiological function	recombinant PtsA and anti-rPtsA antiserum inhibit adhesion of Streptococcus pneumoniae to cultured human lung adenocarcinoma A549 cells, epitope screening, overview. Homologous sequences are found in human BMPER, multimerin1, protocadherin19, integrinbeta4, epsin1 and collagen type VIIalpha1 proteins, all of which can be found in A549 cells except the latter. anti-rPtsA Antiserum reduces bacterial virulence in the intravenous inoculation mouse model. The surface-localized PtsA functions as an adhesin	Streptococcus pneumoniae