|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|BPT5:DIT||Cakate1, Team Purple-A||2017-04-07 13:15:47 CDT||GO:0098025 virus tail, baseplate (C)||PMID:24155371||IDA|
Immunoelectron microscopy images displayed in Figure 1 show the pb9 protein localized in the upper part of the tail of the T5 phage. Through the use of IgG crosslinking, pb9 is proposed to be part of the adsorption device in the baseplate of the virus tail.
|9CAUD:Q9G097||Cakate1, Team Purple-A||2017-04-09 20:01:24 CDT||GO:0098026 virus tail, tube (C)||PMID:27824135||IMP|
A series of different mutations were made in the TMP of this phage, including in the N-termini, C-termini, and hydrophobic regions of the protein. Figure 2 shows that mutations in the N and C-termini resulted in abnormal phage assembly, and hydrophobic region mutations resulted in tail length reduction. Therefore, the TMP is determined to be an important part of the tube in the viral tail.
|9CAUD:R4JMG7||Cakate1, Team Purple-A||2017-04-09 20:21:18 CDT||GO:0008233 peptidase activity (F)||PMID:27637947||IDA|
The M15A peptidase is shown to have peptidase lytic activity against E.coli host cells. Figure 3 shows peptidase activity by plotting it against the optical density of the host cells. The data shows a large reduction in the turbidity of the host cells through the activity of the M15A protein.
|9CAUD:H2D0G4||Cakate1, Team Purple-A||2017-04-09 20:45:04 CDT||GO:0016787 hydrolase activity (F)||PMID:22289622||IDA|
In one of the experiments described, they performed an endolysin assay to test the antimicrobial spectrum of this protein. Table 2 displays the relative lysis activity of SPN1S against certain Gram-positive and Gram-negative bacterial strains. The table shows SPN1S's high relative lysis activity against all the E.coli strains. These results provide evidence that the SPN1S protein has a hydrolase function.
|BPT5:DECO||Cakate1, Team Purple-A||2017-04-12 09:52:53 CDT||GO:0098021 viral capsid, decoration (C)||PMID:28165000||IDA|
An association assay was performed to test the decoration capabilities of pb10 on the T5 capsid. Figure 4 shows that the N-terminal domain of pb10 is responsible for interacting with the capsid. Figure 5 further exhibits a high affinity between the protein and the capsid through an SPR experiment. Overall, these data provide evidence for the decorating capabilities of pb10.
|BPT5:HEL10||Cakate1, Team Purple-A||2017-04-17 10:47:21 CDT||GO:0032508 DNA duplex unwinding (P)||PMID:28009009||IDA|
Figure 3 shows how d10 protein functions to unwind DNA. It uses partially homologous Holliday junction substrates and results in two products, including fork DNA and recombined duplex DNA. These gels prove that d10 can act as a DNA helicase.
|STAA8:Q2G2U2||Endres1, Team Purple-A||2017-04-19 10:52:57 CDT||GO:1900231 regulation of single-species biofilm formation on inanimate substrate (P)||PMID:26406329||IMP|
In Figure 1C it is shown that when knocking out the gene YycL, biofilm production on an inert polystyrene surface greatly increased, showing that YycL has a role in the regulation of biofilm production.
|STAA8:LRGB||Endres1, Team Purple-A||2017-04-19 10:53:54 CDT||GO:1900231 regulation of single-species biofilm formation on inanimate substrate (P)||PMID:26406329||IMP|
In Figure 1A it is shown that when knocking out the gene LrgB, biofilm production on an inert polystyrene surface greatly increased, showing that LrgB has a role in the regulation of biofilm production.
|BPP2:HOLIN||Cakate1, Team Purple-A||2017-04-26 10:09:38 CDT||GO:0034290 holin activity (F)||PMID:23335412||IDA|
Figure 2 displays the results of expressing the holin gene in the lambda phage and testing its lysing abilities on E.coli. The activity assay shows that the holin reduces turbidity in the E.coli and thereby has the lytic properties of a holin.
|BPP2:ANTIH||Cakate1, Team Purple-A||2017-04-26 10:16:10 CDT||GO:1901218 negative regulation of holin activity (P)||PMID:23335412||IDA|
Figure 4B shows the results of expressing the LysA gene on the activity of the Y holin. The incorporation of LysA resulted in a delay of the lysis activity of holin Y, thus indicating its negative regulation.