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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_02502
- pan locus tag?: SAUPAN005692000
- symbol: rplN
- pan gene symbol?: rplN
- synonym:
- product: 50S ribosomal protein L14
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920878 NCBI
- RefSeq: YP_500969 NCBI
- BioCyc: G1I0R-2365 BioCyc
- MicrobesOnline: 1290940 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
61
121
181
241
301
361ATGATCCAACAAGAAACACGCTTGAAAGTAGCAGACAACTCTGGTGCTCGTGAAGTTCTT
ACAATCAAAGTATTAGGTGGATCTGGTCGTAAAACAGCAAACATCGGCGATGTTATCGTA
TGTACTGTTAAAAATGCAACACCAGGTGGCGTTGTTAAAAAAGGTGACGTTGTCAAAGCT
GTAATCGTACGTACTAAGTCAGGTGTTCGTCGTAATGACGGTTCATACATCAAATTTGAT
GAAAATGCATGTGTTATCATCCGTGATGACAAAGGCCCACGTGGTACTCGTATCTTCGGA
CCTGTTGCTCGTGAATTACGTGAAGGTAACTTCATGAAAATCGTATCATTAGCACCAGAA
GTACTTTAA60
120
180
240
300
360
369
⊟Protein[edit | edit source]
Protein Data Bank: 4WCE
Protein Data Bank: 4WF9
Protein Data Bank: 4WFA
Protein Data Bank: 4WFB
Protein Data Bank: 5HKV
Protein Data Bank: 5HL7
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5NRG
Protein Data Bank: 5TCU
⊟General[edit | edit source]
- locus tag: SAOUHSC_02502
- symbol: RplN
- description: 50S ribosomal protein L14
- length: 122
- theoretical pI: 10.7254
- theoretical MW: 13135.2
- GRAVY: -0.141803
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL14 (TIGR01067; HMM-score: 192.3)and 1 more50S ribosomal protein uL14 (TIGR03673; HMM-score: 96.6)
- TheSEED :
- LSU ribosomal protein L14p (L23e)
- PFAM: no clan defined Ribosomal_L14; Ribosomal protein L14p/L23e (PF00238; HMM-score: 180.3)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 10
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0
- Extracellular Score: 0
- 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): 0.091516
- TAT(Tat/SPI): 0.009224
- LIPO(Sec/SPII): 0.006493
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MIQQETRLKVADNSGAREVLTIKVLGGSGRKTANIGDVIVCTVKNATPGGVVKKGDVVKAVIVRTKSGVRRNDGSYIKFDENACVIIRDDKGPRGTRIFGPVARELREGNFMKIVSLAPEVL
⊟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_01170 (carB) carbamoyl phosphate synthase large subunit [4] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [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_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [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_00020 two-component response regulator [4] (data from MRSA252) SAOUHSC_00153 indolepyruvate decarboxylase [4] (data from MRSA252) SAOUHSC_00472 ribose-phosphate pyrophosphokinase [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_00562 phosphomethylpyrimidine kinase [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00742 ribonucleotide-diphosphate reductase subunit alpha [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_00906 hypothetical protein [4] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01451 threonine dehydratase [4] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01814 hypothetical protein [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_01820 acetate kinase [4] (data from MRSA252) SAOUHSC_01909 S-adenosylmethionine synthetase [4] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [4] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252) SAOUHSC_02965 carbamate kinase [4] (data from MRSA252) SAOUHSC_02969 arginine deiminase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟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 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 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)