PMID:8943245 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:56:17Z

change PMID template to TableEdit version

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	'''~~No author listed~~''' (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. ''J. Biol. Chem.'' '''271''':31981-8		'''Fan, F and Macnab, RM''' (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. ''J. Biol. Chem.'' '''271''':31981-8
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imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:53:45Z

change PMID template to TableEdit version

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	~~<span style~~ = ~~'font-size: large'>~~ '''~~Fan, F and Macnab, RM~~''' (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.''J. Biol. Chem.'' '''271''':31981-8</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. ''J. Biol. Chem.'' '''271''':31981-8
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			!align=left \|Abstract
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			FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, which was fully functional in complementation tests, was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM; Mg2+ was required. The activity was not affected by inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8943245 PubMed]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|\| FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, ~~which was fully functional in complementation tests~~, ~~was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM~~; ~~Mg2+ was required. The activity was not affected by inhibitors of the F-~~, V- ~~or P~~-~~type~~ ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Adenosine Diphosphate/metabolism; Adenosine Triphosphatases/metabolism; Bacterial Proteins; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Genetic Complementation Test; Mutagenesis, Site-Directed; Proteins/chemistry; Proton-Translocating ATPases; Rosaniline Dyes; Salmonella typhimurium; Temperature
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~8943245 PubMed~~]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

127.0.0.1: /Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

2010-06-17T21:21:37Z

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127.0.0.1: Update TableEdit tables.

2010-01-09T05:05:04Z

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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T07:46:04Z

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127.0.0.1: Edited by wikibot

2008-04-30T11:55:00Z

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127.0.0.1: Edited by wikibot

2008-04-25T22:03:42Z

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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

66.249.70.172: New PMID: Page!

2007-07-24T17:14:42Z

New PMID: Page!

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<span style = 'font-size: large'> '''Fan, F and Macnab, RM''' (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.''J. Biol. Chem.'' '''271''':31981-8</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, which was fully functional in complementation tests, was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM; Mg2+ was required. The activity was not affected by inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8943245 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>
[{{SERVER}}/colipedia/index.php/Special:TableEdit?id=63ce1649aab8b3180235b0af7618f667.0.Q46a63382ed9fc&page=0&pagename={{FULLPAGENAMEE}}&type=0 Add GO annotations]
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>