hflC:Quickview: Difference between revisions
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{| | {| id="V49aee8abdac57" class=" tableEdit New_Quickview_Table" | ||
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Standard Name | ||
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''hflC'' | |||
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Gene Synonym(s) | ||
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''ECK4171, b4175, JW4133, hflA''<ref name='LIB:Riley_2006'/>, hflA'' | |||
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Product Desc. | ||
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regulator of FtsH protease<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/> | regulator of FtsH protease<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>; | ||
Component of [[:Category:Complex:HflK-HflC complex; regulator of FtsH protease|HflK-HflC complex; regulator of FtsH protease]]<ref name='LIB:EcoCyc11.1'/> | Component of [[:Category:Complex:HflK-HflC complex; regulator of FtsH protease|HflK-HflC complex; regulator of FtsH protease]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:HflB, integral membrane ATP-dependent zinc metallopeptidase|HflB, integral membrane ATP-dependent zinc metallopeptidase]]<ref name='LIB:EcoCyc11.1'/> | ||
Membrane bound protease complex, with FtsH and HflK; regulates lysogeny; non-essential<ref name='LIB:EcoGene'/> | |||
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!align=left {{table_heading_style}} |Knock-Out Phenotype | !align=left {{table_heading_style}} |Product Synonyms(s) | ||
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''modulator for HflB protease specific for phage lambda cII repressor<ref name='LIB:Riley_2006'/>, B4175<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HflA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HflC<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> , ECK4171, hflA, JW4133, b4175'' | |||
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!align=left {{table_heading_style}} |Function from GO | |||
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<GO_nr /> | |||
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!align=left {{table_heading_style}} |Knock-Out Phenotype | |||
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!align=left {{table_heading_style}} |Regulation/Expression | !align=left {{table_heading_style}} |Regulation/Expression | ||
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transcription unit(s): [[:Category:Txn_unit:yjeFE-amiB-mutL-miaA-hfq-hflXKC|yjeFE-amiB-mutL-miaA-hfq-hflXKC]]<ref name='LIB:EcoCyc10.6'/>, ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC | transcription unit(s): [[:Category:Txn_unit:yjeFE-amiB-mutL-miaA-hfq-hflXKC|yjeFE-amiB-mutL-miaA-hfq-hflXKC]]<ref name='LIB:EcoCyc10.6'/>, ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC | ||
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!align=left {{table_heading_style}} |Quick Links | |||
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[[File:porteco.png|link=http://porteco.org/AjaxSearch.jsp?searchString=hflC&s=search]] [[File:EcoCyc.gif|link=http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG10435]] [[File:regulondb.jpg|link=http://regulondb.ccg.unam.mx/gene?term=ECK120000428&organism=ECK12&format=jsp&type=gene ]] <br/><br/> [[File:dnadisplay.png|link=http://ecoliwiki.net/tools/display_dna.php?gene=hflC&loc=MG1655%3A4401323..4402327,W3110%3A4407980..4408984,REL606%3A4381455..4382459,DH10B%3A4501685..4502689,BW2952%3A4340058..4341062]] [[File:proteindisplay.png|link=http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=4340058&end=4341062&gene=hflC&aa=mrksviaiiiivlvvlymsvfvvkegergitlrfgkvlrdddnkplvyepglhfkipfietvkmldariqtmdnqadrfvtkekkdlivdsyikwrisdfsryylatgggdisqaevllkrkfsdrlrseigrldvkdivtdsrgrltlevrdalnsgsagtedevttpaadnaiaeaaervtaetkgkvpvinpnsmaalgievvdvrikqinlptevseaiynrmraereavarrhrsqgqeeaeklratadyevtrtlaeaerqgrimrgegdaeaaklfadafskdpdfyafirslrayensfsgnqdvmvmspdsdffrymktptsatr]] [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=hflC+AND+escherichia+coli]] [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=hflC]] | |||
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{{Quickview_table_help}} | {{Quickview_table_help}} | ||
<protect><!--Quickview_notes--></protect> | <protect><!--Quickview_notes--></protect> | ||
===Notes=== | ===Notes=== | ||
{{BacktoTop}} | {{BacktoTop}} | ||
Gain-of-function alleles in hflC and hflK inhibit FtsH-mediated degradation of uncomplexed SecY protein and other membrane protein substrates. Null hflC or hflK alleles stabilize cytoplasmic substrate cII. hflCK is a multicopy suppressor of ftsH htpX double mutant. Serine protease-like motif in HflC not required for cII degradation. HflC and HflK have a periplasmic prohibitin homology (PHB) domain. HT_Cmplx45_Mem: HflC+HybC+BamB.<ref name='LIB:EcoGene'/> | |||
Latest revision as of 21:54, 27 May 2013
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
| Standard Name |
hflC |
|---|---|
| Gene Synonym(s) |
ECK4171, b4175, JW4133, hflA[1], hflA |
| Product Desc. |
regulator of FtsH protease[2][3]; Component of HflK-HflC complex; regulator of FtsH protease[3]; HflB, integral membrane ATP-dependent zinc metallopeptidase[3] Membrane bound protease complex, with FtsH and HflK; regulates lysogeny; non-essential[4] |
| Product Synonyms(s) |
modulator for HflB protease specific for phage lambda cII repressor[1], B4175[2][1], HflA[2][1], HflC[2][1] , ECK4171, hflA, JW4133, b4175 |
| Function from GO |
<GO_nr /> |
| Knock-Out Phenotype | |
| Regulation/Expression |
transcription unit(s): yjeFE-amiB-mutL-miaA-hfq-hflXKC[2], ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC |
| Regulation/Activity | |
| Quick Links | |
| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
Gain-of-function alleles in hflC and hflK inhibit FtsH-mediated degradation of uncomplexed SecY protein and other membrane protein substrates. Null hflC or hflK alleles stabilize cytoplasmic substrate cII. hflCK is a multicopy suppressor of ftsH htpX double mutant. Serine protease-like motif in HflC not required for cII degradation. HflC and HflK have a periplasmic prohibitin homology (PHB) domain. HT_Cmplx45_Mem: HflC+HybC+BamB.[4]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.


