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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]

Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    GTGCACATCGTGGCTAAAAAAGTAGATAAAGTTGTTAAATTACAAATTCCTGCAGGTAAA
    GCGAATCCAGCACCACCAGTTGGTCCAGCATTAGGTCAAGCAGGTGTGAACATCATGGGA
    TTCTGTAAAGAGTTCAATGCACGTACTCAAGATCAAGCAGGTTTAATTATTCCGGTAGAA
    ATCAGTGTTTATGAAGATCGTTCATTTACATTTATTACAAAAACTCCACCGGCTCCAGTA
    TTACTTAAAAAAGCAGCTGGTATTGAAAAAGGTTCAGGCGAACCAAACAAAACTAAAGTT
    GCTACAGTAACTAAAAATCAAGTACGCGAAATTGCTAACAGCAAAATGCAAGACTTAAAC
    GCTGCTGACGAAGAAGCAGCTATGCGTATTATCGAAGGTACTGCACGTAGTATGGGTATC
    GTTGTAGAATAA
    60
    120
    180
    240
    300
    360
    420
    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:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL11 (TIGR01632; HMM-score: 215.2)
  • TheSEED  :
    • LSU ribosomal protein L11p (L12e)
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  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)
    SACOL0815ribosomal subunit interface protein  [7] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [7] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [7] (data from MRSA252)
    SACOL2535D-lactate dehydrogenase  [7] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [7] (data from MRSA252)

Expression & Regulation[edit | edit source]

Regulation[edit | edit source]

  • regulator:

Transcription pattern[edit | edit source]

Protein synthesis (provided by Aureolib)[edit | edit source]

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]

  1. 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)
  2. 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)
  3. 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)
  4. 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)
  5. 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)
  6. 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. 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)
  8. 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)

Relevant publications[edit | edit source]