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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0583 [new locus tag: SACOL_RS03025 ]
- pan locus tag?: SAUPAN002307000
- symbol: rplK
- pan gene symbol?: rplK
- synonym:
- product: 50S ribosomal protein L11
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0583 [new locus tag: SACOL_RS03025 ]
- symbol: rplK
- product: 50S ribosomal protein L11
- replicon: chromosome
- strand: +
- coordinates: 603476..603907
- length: 432
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236218 NCBI
- RefSeq: YP_185469 NCBI
- BioCyc: see SACOL_RS03025
- MicrobesOnline: 912063 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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421GTGCACATCGTGGCTAAAAAAGTAGATAAAGTTGTTAAATTACAAATTCCTGCAGGTAAA
GCGAATCCAGCACCACCAGTTGGTCCAGCATTAGGTCAAGCAGGTGTGAACATCATGGGA
TTCTGTAAAGAGTTCAATGCACGTACTCAAGATCAAGCAGGTTTAATTATTCCGGTAGAA
ATCAGTGTTTATGAAGATCGTTCATTTACATTTATTACAAAAACTCCACCGGCTCCAGTA
TTACTTAAAAAAGCAGCTGGTATTGAAAAAGGTTCAGGCGAACCAAACAAAACTAAAGTT
GCTACAGTAACTAAAAATCAAGTACGCGAAATTGCTAACAGCAAAATGCAAGACTTAAAC
GCTGCTGACGAAGAAGCAGCTATGCGTATTATCGAAGGTACTGCACGTAGTATGGGTATC
GTTGTAGAATAA60
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432
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0583 [new locus tag: SACOL_RS03025 ]
- symbol: RplK
- description: 50S ribosomal protein L11
- length: 143
- theoretical pI: 9.92996
- theoretical MW: 15222.6
- GRAVY: -0.128671
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL11 (TIGR01632; HMM-score: 215.2)
- TheSEED :
- LSU ribosomal protein L11p (L12e)
- PFAM: no clan defined Ribosomal_L11_N; Ribosomal protein L11, N-terminal domain (PF03946; HMM-score: 108.4)Ribosomal_L11; Ribosomal protein L11, RNA binding domain (PF00298; HMM-score: 87.1)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- 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): 0.04089
- TAT(Tat/SPI): 0.002918
- LIPO(Sec/SPII): 0.00627
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MHIVAKKVDKVVKLQIPAGKANPAPPVGPALGQAGVNIMGFCKEFNARTQDQAGLIIPVEISVYEDRSFTFITKTPPAPVLLKKAAGIEKGSGEPNKTKVATVTKNQVREIANSKMQDLNAADEEAAMRIIEGTARSMGIVVE
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4] [5]
- quantitative data / protein copy number per cell: 2823 [6]
- interaction partners:
SACOL1760 (ackA) acetate kinase [7] (data from MRSA252) SACOL1385 (acnA) aconitate hydratase [7] (data from MRSA252) SACOL0660 (adhP) alcohol dehydrogenase [7] (data from MRSA252) SACOL0452 (ahpC) alkyl hydroperoxide reductase subunit C [7] (data from MRSA252) SACOL2657 (arcA) arginine deiminase [7] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [7] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [7] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [7] (data from MRSA252) SACOL2117 (fbaA) fructose-bisphosphate aldolase [7] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [7] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [7] (data from MRSA252) SACOL1782 (fhs) formate--tetrahydrofolate ligase [7] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [7] (data from MRSA252) SACOL0593 (fusA) elongation factor G [7] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [7] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [7] (data from MRSA252) SACOL0961 (gluD) glutamate dehydrogenase [7] (data from MRSA252) SACOL2415 (gpmA) phosphoglyceromutase [7] (data from MRSA252) SACOL2017 (groES) co-chaperonin GroES [7] (data from MRSA252) SACOL0460 (guaB) inosine-5'-monophosphate dehydrogenase [7] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [7] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [7] (data from MRSA252) SACOL0240 (ispD) 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [7] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [7] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [7] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [7] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [7] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [7] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [7] (data from MRSA252) SACOL1746 (pfkA) 6-phosphofructokinase [7] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [7] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [7] (data from MRSA252) SACOL0839 (pgk) phosphoglycerate kinase [7] (data from MRSA252) SACOL1982 (ppaC) manganese-dependent inorganic pyrophosphatase [7] (data from MRSA252) SACOL1092 (ptsI) phosphoenolpyruvate-protein phosphotransferase [7] (data from MRSA252) SACOL2119 (pyrG) CTP synthetase [7] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [7] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [7] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [7] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [7] (data from MRSA252) SACOL2229 (rplN) 50S ribosomal protein L14 [7] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [7] (data from MRSA252) SACOL2212 (rplQ) 50S ribosomal protein L17 [7] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [7] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [7] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [7] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [7] (data from MRSA252) SACOL0545 (rplY) 50S ribosomal protein L25/general stress protein Ctc [7] (data from MRSA252) SACOL1700 (rpmA) 50S ribosomal protein L27 [7] (data from MRSA252) SACOL2112 (rpmE2) 50S ribosomal protein L31 [7] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [7] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [7] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [7] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [7] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [7] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [7] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [7] (data from MRSA252) SACOL1254 (rpsP) 30S ribosomal protein S16 [7] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [7] (data from MRSA252) SACOL0009 (serS) seryl-tRNA synthetase [7] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [7] (data from MRSA252) SACOL1262 (sucC) succinyl-CoA synthetase subunit beta [7] (data from MRSA252) SACOL1263 (sucD) succinyl-CoA synthetase subunit alpha [7] (data from MRSA252) SACOL1722 (tig) trigger factor [7] (data from MRSA252) SACOL0840 (tpiA) triosephosphate isomerase [7] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [7] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [7] (data from MRSA252) SACOL0815 ribosomal subunit interface protein [7] (data from MRSA252) SACOL0944 NADH dehydrogenase [7] (data from MRSA252) SACOL2173 alkaline shock protein 23 [7] (data from MRSA252) SACOL2535 D-lactate dehydrogenase [7] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [7] (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: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: 18.31 h [8]
⊟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]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ Annette Dreisbach, Kristina Hempel, Girbe Buist, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
Profiling the surfacome of Staphylococcus aureus.
Proteomics: 2010, 10(17);3082-96
[PubMed:20662103] [WorldCat.org] [DOI] (I p) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑ 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 7.11 7.12 7.13 7.14 7.15 7.16 7.17 7.18 7.19 7.20 7.21 7.22 7.23 7.24 7.25 7.26 7.27 7.28 7.29 7.30 7.31 7.32 7.33 7.34 7.35 7.36 7.37 7.38 7.39 7.40 7.41 7.42 7.43 7.44 7.45 7.46 7.47 7.48 7.49 7.50 7.51 7.52 7.53 7.54 7.55 7.56 7.57 7.58 7.59 7.60 7.61 7.62 7.63 7.64 7.65 7.66 7.67 7.68 7.69 7.70 7.71 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) - ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)