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User:Ortizvi3

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SUPER BOWL (Round 5)

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
acceptableBACAM:D2D3C32012-04-10 22:19:19 CDTGO:0008233 peptidase activity (F)PMID:21617349ECO:0000314 direct assay evidence used in manual assertion

Direct Assay Evidence Code was inferred based on Figure 3: SDS-PAGE (left) and fibrin zymogram (right) of culture supernatant, which shows bands of 90, 55, and 40 kDa of B. subtilis TF (cells harboring pHYbpr86-1) that were likely derived from bacillopeptidse F.

challenge
acceptableSTRP1:Q9A1742012-04-13 15:32:13 CDTGO:0016757 transferase activity, transferring glycosyl groups (F)PMID:15458407ECO:0000315 mutant phenotype evidence used in manual assertion

Mutant phenotype was inferred based on Figure 4, in which SpyA was assayed for the ability to ADP-ribosylate arginine.

As shown, there was labelled precipitated material when SpyA was incubated with poly-l-arginine and only limited precipitated radioactive material with the active site mutant SpyA-E187A.

challenge
acceptableSTREE:B0BD082012-04-13 16:55:56 CDTGO:0004674 protein serine/threonine kinase activity (F)PMID:20453092ECO:0000315 mutant phenotype evidence used in manual assertion

Mutant Phenotype was inferred based on Figure 1: Detection of in vivo phosphorylated proteins in S. pneumoniae. Cell lysates from cultures of a wild-type strain of S. pneumoniae (Sp1) and a ΔstkP mutant strain (Sp10) were immuno-labeled and the patterns of phosphorylated proteins in the cytoplasmic and membrane fractions were compared.

The anti-pThr antibody reacted with at least six protein bands in the wild type; however, no phosphorylated proteins were detected in the Sp10 strain. This result indicated that phosphorylation on Thr residues in S. pneumoniae is dependent on the presence of StkP.

challenge
requireschangesSTRGC:A8AXP32012-04-15 10:54:15 CDTGO:0016787 hydrolase activity (F)PMID:22123253ECO:0000315 mutant phenotype evidence used in manual assertion

Mutant Phenotype was deduced based on Table 3: Impact of LytF on the efficiency of gene transfer from donor to recipient cells during co-cultivation. The table strongly indicates that LytF causes lysis of AH2 target cells (hydrolase activity), followed by release of DNA that can be taken up by competent SGH25 cells.

challenge

acceptable:3
unacceptable:0
requires_changes:1
flagged:0

Annotations challenged by Ortizvi3

StatusAuthor,GroupPageGO Term (Aspect)ReferenceEvidenceLinksPage history

0 annotations fixed by Ortizvi3


MSU Internal

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
acceptableLACCA:Q840T22012-03-30 17:35:34 CDTGO:0034338 short-chain carboxylesterase activity (F)PMID:15184114ECO:0000314 direct assay evidence used in manual assertion

IDA is supported by Fig 5. Overexpression of esterase from Lactobacillus casei CL96 in E. coli BL21(DE3)/pLysS. A polypeptide with a molecular mass of about 68 kDa and esterase activity was produced, in agreement with

the calculated molecular mass of the predicted amino acid sequence.

challenge
acceptableLACCA:Q5H7T02012-03-30 19:43:57 CDTGO:0051670 inulinase activity (F)PMID:22197658ECO:0000314 direct assay evidence used in manual assertion

IDA based on evidence showed on Fig. 4.

Cloning of the LevH1 enzyme catalytic region in E. coli XL1. Different protein profiles were constructed based on LevH1 gene. The enzymatic activity of the pKNL1 recombinant plasmid suggests that both, variable and catalytic domains, are essential for LevH1 inulinase activity.

challenge
requireschangesLACRG:C7T9C62012-03-30 22:04:18 CDTGO:0004175 endopeptidase activity (IMP based on evidence showed on Fig. 2.

Phase-contrast (A,B&C) and Transmission Electron Microscopy (TEM) pictures (D&E) of LGG wild-type (A&D), msp1 mutant cells CMPG10200 (B&E) and plasmid-complemented CMPG10203 cells (C).

The msp1 knock-out mutant shows a defect in cell separation as visualized by phase contrast and electron microscopy. Plasmid-mediated complementation of the mutant restored the wild-type phenotype. )
PMID:22359601IMP: Inferred from Mutant Phenotype
challenge
requireschangesCAMJE:LUXS2012-04-01 00:34:03 CDTGO:0043768 S-ribosylhomocysteine lyase activity (F)PMID:11988522ECO:0000315 mutant phenotype evidence used in manual assertion

IMP based on Fig. 2 and Figure 3 evidence; Figure 2 shows the production of an extracellular signalling molecule with AI-2-like activity by C. jejuni NCTC 11168; Figure 3 shows that Cj1198 can generate AI-2-like activity in a heterologous host when the addition of cell-free culture medium from cells containing pKE25 stimulated luminescence in a manner similar to the positive control (V. harveyi BB152).

challenge
acceptableLACLM:A2RI962012-04-01 00:32:45 CDTGO:0003755 peptidyl-prolyl cis-trans isomerase activity (F)PMID:22442694ECO:0000314 direct assay evidence used in manual assertion

IDA based on Figure 2 evidence, in which a recombinant soluble form of PpiA that had been produced and secreted in L. lactis and purified from a culture supernatant displayed both PPIase and chaperone activities.

challenge
requireschangesSTRSU:A5JSI32012-03-31 22:25:38 CDTGO:0008745 N-acetylmuramoyl-L-alanine amidase activity (F)PMID:22228730ECO:0000315 mutant phenotype evidence used in manual assertion

IMP was demonstrated based on Figure 2, which shows autolysin profile of wild type and complementation strain. The lytic pattern was absent in the mutant strain.

challenge
acceptableLACLM:XERS2012-04-01 00:28:39 CDTGO:0009037 tyrosine-based site-specific recombinase activity (F)PMID:17630835ECO:0000315 mutant phenotype evidence used in manual assertion

IMP was conclude based on Figure 3, which indicates XerS/difSL Recombination in E. coli. In absence of the lactococcal XerS recombinase, almost no recombination was observed indicating that XerCD of E. coli do not recombine difSL. In contrast, introduction of a plasmid expressing the lactococcal xerS gene increased the excision frequency (observed in E. coli when using the native XerCD/dif system.)

challenge

acceptable:4
unacceptable:0
requires_changes:3
flagged:0

Annotations challenged by Ortizvi3

StatusAuthor,GroupPageGO Term (Aspect)ReferenceEvidenceLinksPage history

0 annotations fixed by Ortizvi3