pagP:Quickview: Difference between revisions
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!align=left | !align=left {{table_heading_style}} |Standard Name | ||
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''pagP'' | ''pagP'' | ||
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!align=left | !align=left {{table_heading_style}} |Gene Synonym(s) | ||
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''crcA, ECK0615, b0622, JW0617, ybeG''<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/> | ''crcA, ECK0615, b0622, JW0617, ybeG''<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/> | ||
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!align=left | !align=left {{table_heading_style}} |Product Desc. | ||
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PagP<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>; | PagP<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>; | ||
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Lipid A biosynthesis, outer membrane; transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A (or its precursors); confers resistance to cationic antimicrobial peptides<ref name='LIB:EcoGene'/> | Lipid A biosynthesis, outer membrane; transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A (or its precursors); confers resistance to cationic antimicrobial peptides<ref name='LIB:EcoGene'/> | ||
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!align=left | !align=left {{table_heading_style}} |Product Synonyms(s) | ||
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palmitoyl transferase for Lipid A<ref name='LIB:Riley_2006'/>, B0622<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YbeG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CrcA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, PagP<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | palmitoyl transferase for Lipid A<ref name='LIB:Riley_2006'/>, B0622<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YbeG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CrcA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, PagP<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | ||
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!align=left | !align=left {{table_heading_style}} |Function from GO | ||
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!align=left | !align=left {{table_heading_style}} |Knock-Out Phenotype | ||
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!align=left {{table_heading_style}} |Regulation/Expression | |||
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transcription unit(s): [[:Category:Txn_unit:pagP|pagP]]<ref name='LIB:EcoCyc10.6'/>, crcA | transcription unit(s): [[:Category:Txn_unit:pagP|pagP]]<ref name='LIB:EcoCyc10.6'/>, crcA | ||
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!align=left | !align=left {{table_heading_style}} |Regulation/Activity | ||
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!align=left {{table_heading_style}} |Quick Links | |||
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[http://ecoliwiki.net/tools/display_dna.php?gene=pagP&loc=MG1655:655780..656340,W3110:656979..657539 DNA display] [http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=656979&end=657539&gene=pagP&aa=mnvskyvaifsfvfiqlisvgkvfanadewmttfreniaqtwqqpehydlyipaitwharfaydkektdrynerpwgggfglsrwdekgnwhglyamafkdswnkwepiagygwestwrpladenfhlglgftagvtardnwnyiplpvllplasvgygpvtfqmtyipgtynngnvyfawmrfqf Protein display] [http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=pagP+AND+escherichia+coli Pubmed(pagP)] [http://trimer.tamu.edu/cgi-bin/textpresso/2.1/ecoli/search?searchstring=pagP Textpresso(pagP)] | |||
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Revision as of 23:37, 21 January 2010
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
See Help:Quickview for help with entering information in the Quickview table.
| Standard Name |
pagP |
|---|---|
| Gene Synonym(s) | |
| Product Desc. |
Component of palmitoyl transferase for Lipid A[3] Lipid A biosynthesis, outer membrane; transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A (or its precursors); confers resistance to cationic antimicrobial peptides[4] |
| Product Synonyms(s) |
palmitoyl transferase for Lipid A[1], B0622[2][1], YbeG[2][1], CrcA[2][1], PagP[2][1] |
| Function from GO | |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity | |
| Quick Links | |
| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
Mg(2+) stimulon-PhoPQ regulon, EvgAS-PhoPQ cascade enhanced-expression subset. The phoP-activation phenotype (PagP) was initially characterized in Salmonella then confirmed in E. coli (Jia, 2004). SignalP-NN incorrectly predicts a 27 aa signal peptide, but the verified cleavage site after 25 aa is predicted as a second possible cleavage site by SignalP-NN and as the only cleavage site by the more recent SignalP-HMM predictor (see SignalP button below).[4]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 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 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 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.