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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01203
- pan locus tag?: SAUPAN003520000
- symbol: rnc
- pan gene symbol?: rnc
- synonym:
- product: ribonuclease III
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3919469 NCBI
- RefSeq: YP_499740 NCBI
- BioCyc: G1I0R-1127 BioCyc
- MicrobesOnline: 1289654 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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721ATGTCTAAACAAAAGAAAAGTGAGATAGTTAATCGTTTTAGAAAGCGCTTTGATACTAAA
ATGACAGAGTTAGGCTTTACTTATCAAAATATTGATTTATACCAACAAGCATTTTCGCAT
TCGAGTTTTATTAATGATTTTAATATGAATCGTTTAGACCATAATGAGCGTTTAGAGTTT
TTGGGTGATGCGGTATTAGAATTGACGGTTTCACGATATTTATTTGATAAACATCCCAAC
TTGCCAGAAGGGAATTTAACAAAAATGCGTGCCACTATTGTATGTGAGCCCTCACTTGTA
ATATTTGCGAATAAAATTGGATTGAACGAAATGATTTTACTTGGTAAAGGTGAAGAGAAA
ACAGGGGGACGTACAAGACCATCATTAATATCAGATGCATTCGAAGCATTTATTGGGGCA
TTGTATTTGGATCAAGGACTAGATATAGTTTGGAAATTTGCTGAGAAAGTCATTTTCCCA
CATGTAGAACAAAATGAGTTATTAGGCGTGGTAGATTTTAAAACACAATTCCAAGAATAT
GTGCACCAGCAAAATAAAGGTGATGTAACCTATAATTTAATAAAAGAAGAGGGACCGGCA
CATCATCGTCTATTCACTTCAGAAGTTATTCTGCAAGGGGAAGCAATAGCTGAAGGTAAA
GGGAAAACGAAAAAAGAATCAGAACAACGTGCTGCTGAAAGTGCCTATAAGCAATTAAAA
CAAATTAAATAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01203
- symbol: Rnc
- description: ribonuclease III
- length: 243
- theoretical pI: 7.23578
- theoretical MW: 27921.6
- GRAVY: -0.493416
⊟Function[edit | edit source]
- reaction: EC 3.1.26.3? ExPASyRibonuclease III Endonucleolytic cleavage to 5'-phosphomonoester
- TIGRFAM: Transcription RNA processing ribonuclease III (TIGR02191; EC 3.1.26.3; HMM-score: 266.4)and 1 moreseadornavirus double-stranded RNA-binding protein (TIGR04238; HMM-score: 17.2)
- TheSEED :
- Ribonuclease III (EC 3.1.26.3)
Cell Division and Cell Cycle Cell Division and Cell Cycle - no subcategory Two cell division clusters relating to chromosome partitioning Ribonuclease III (EC 3.1.26.3)and 1 more - PFAM: RNase_III (CL0539) Ribonucleas_3_3; Ribonuclease-III-like (PF14622; HMM-score: 124.2)and 2 moreRibonuclease_3; Ribonuclease III domain (PF00636; HMM-score: 78.7)DSRM (CL0196) dsrm; Double-stranded RNA binding motif (PF00035; HMM-score: 60.1)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Mg2+
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.004111
- TAT(Tat/SPI): 0.000265
- LIPO(Sec/SPII): 0.000429
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MSKQKKSEIVNRFRKRFDTKMTELGFTYQNIDLYQQAFSHSSFINDFNMNRLDHNERLEFLGDAVLELTVSRYLFDKHPNLPEGNLTKMRATIVCEPSLVIFANKIGLNEMILLGKGEEKTGGRTRPSLISDAFEAFIGALYLDQGLDIVWKFAEKVIFPHVEQNELLGVVDFKTQFQEYVHQQNKGDVTYNLIKEEGPAHHRLFTSEVILQGEAIAEGKGKTKKESEQRAAESAYKQLKQIK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [2] [3]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_02703 (gpmA) 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [4] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [4] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [4] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [4] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [4] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [4] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [4] (data from MRSA252) SAOUHSC_01788 (thrS) threonyl-tRNA synthetase [4] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [4] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [4] (data from MRSA252) SAOUHSC_00153 indolepyruvate decarboxylase [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [4] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [4] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00488 hypothetical protein [4] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00535 hypothetical protein [4] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00836 glycine cleavage system protein H [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [4] (data from MRSA252) SAOUHSC_01347 aconitate hydratase [4] (data from MRSA252) SAOUHSC_01403 cold shock protein [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_01820 acetate kinase [4] (data from MRSA252) SAOUHSC_01901 putative translaldolase [4] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [4] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: acpP > rnc > SAOUHSC_01204 > SAOUHSC_01205 > SAOUHSC_01206 > SAOUHSC_01207predicted SigA promoter [5] : SAOUHSC_01196 > SAOUHSC_01197 > SAOUHSC_01198 > SAOUHSC_01199 > S494 > S495 > acpP > S496 > rnc > S497 > SAOUHSC_01204 > SAOUHSC_01205 > SAOUHSC_01206 > SAOUHSC_01207 > S498predicted SigA promoter [5] : S495 > acpP > S496 > rnc > S497 > SAOUHSC_01204 > SAOUHSC_01205 > SAOUHSC_01206 > SAOUHSC_01207 > S498
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
BMC Genomics: 2009, 10;291
[PubMed:19570206] [WorldCat.org] [DOI] (I e) - ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p) - ↑ 5.0 5.1 5.2 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)