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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS02905 [old locus tag: SA0495 ]
  • pan locus tag?: SAUPAN002307000
  • symbol: SA_RS02905
  • 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: SA_RS02905 [old locus tag: SA0495 ]
  • symbol: SA_RS02905
  • product: 50S ribosomal protein L11
  • replicon: chromosome
  • strand: +
  • coordinates: 576117..576539
  • length: 423
  • essential: yes [1] DEG other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (576117..576539) NCBI
  • BioCyc: SA_RS02905 BioCyc
  • MicrobesOnline: see SA0495

⊟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
    GTGGCTAAAAAAGTAGATAAAGTTGTTAAATTACAAATTCCTGCAGGTAAAGCGAATCCA
    GCACCACCAGTTGGTCCAGCATTAGGTCAAGCAGGTGTGAACATCATGGGATTCTGTAAA
    GAGTTCAATGCACGTACTCAAGATCAAGCAGGTTTAATTATTCCGGTAGAAATCAGTGTT
    TATGAAGATCGTTCATTTACATTTATTACAAAAACTCCACCGGCTCCAGTATTACTTAAA
    AAAGCAGCTGGTATTGAAAAAGGTTCAGGCGAACCAAACAAAACTAAAGTTGCTACAGTA
    ACTAAAGATCAAGTACGCGAAATTGCTAACAGCAAAATGCAAGACTTAAACGCTGCTGAC
    GAAGAAGCAGCTATGCGTATTATCGAAGGTACTGCACGTAGTATGGGTATCGTTGTAGAA
    TAA
    60
    120
    180
    240
    300
    360
    420
    423

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA_RS02905 [old locus tag: SA0495 ]
  • symbol: SA_RS02905
  • description: 50S ribosomal protein L11
  • length: 140
  • theoretical pI: 9.63296
  • theoretical MW: 14874.2
  • GRAVY: -0.170714

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL11 (TIGR01632; HMM-score: 215.4)
  • TheSEED: see SA0495
  • PFAM:
    no clan defined Ribosomal_L11_N; Ribosomal protein L11, N-terminal domain (PF03946; HMM-score: 108.5)
    Ribosomal_L11; Ribosomal protein L11, RNA binding domain (PF00298; HMM-score: 88.7)

⊟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:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.034995
    • TAT(Tat/SPI): 0.002003
    • LIPO(Sec/SPII): 0.002859
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKKVDKVVKLQIPAGKANPAPPVGPALGQAGVNIMGFCKEFNARTQDQAGLIIPVEISVYEDRSFTFITKTPPAPVLLKKAAGIEKGSGEPNKTKVATVTKDQVREIANSKMQDLNAADEEAAMRIIEGTARSMGIVVE

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA_RS00185serine--tRNA ligase  [2] (data from MRSA252)
    SA_RS00690immunoglobulin G-binding protein A  [2] (data from MRSA252)
    SA_RS01275formate acetyltransferase  [2] (data from MRSA252)
    SA_RS01365L-lactate dehydrogenase  [2] (data from MRSA252)
    SA_RS014452-C-methyl-D-erythritol 4-phosphate cytidylyltransferase  [2] (data from MRSA252)
    SA_RS02095alkyl hydroperoxide reductase subunit C  [2] (data from MRSA252)
    SA_RS02145IMP dehydrogenase  [2] (data from MRSA252)
    SA_RS0265050S ribosomal protein L25/general stress protein Ctc  [2] (data from MRSA252)
    SA_RS02710cysteine synthase  [2] (data from MRSA252)
    SA_RS0291550S ribosomal protein L10  [2] (data from MRSA252)
    SA_RS0292050S ribosomal protein L7/L12  [2] (data from MRSA252)
    SA_RS02935DNA-directed RNA polymerase subunit beta'  [2] (data from MRSA252)
    SA_RS02955elongation factor G  [2] (data from MRSA252)
    SA_RS02960elongation factor Tu  [2] (data from MRSA252)
    SA_RS03250zinc-dependent alcohol dehydrogenase  [2] (data from MRSA252)
    SA_RS04020ribosomal subunit interface protein  [2] (data from MRSA252)
    SA_RS04140aldehyde dehydrogenase  [2] (data from MRSA252)
    SA_RS04145phosphoglycerate kinase  [2] (data from MRSA252)
    SA_RS04150triose-phosphate isomerase  [2] (data from MRSA252)
    SA_RS04160enolase  [2] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [2] (data from MRSA252)
    SA_RS04660NAD-specific glutamate dehydrogenase  [2] (data from MRSA252)
    SA_RS04680glucose-6-phosphate isomerase  [2] (data from MRSA252)
    SA_RS05300phosphoenolpyruvate--protein phosphotransferase  [2] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [2] (data from MRSA252)
    SA_RS05355pyruvate dehydrogenase E1 component subunit beta  [2] (data from MRSA252)
    SA_RS05360dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  [2] (data from MRSA252)
    SA_RS05365dihydrolipoyl dehydrogenase  [2] (data from MRSA252)
    SA_RS05860cell division protein FtsZ  [2] (data from MRSA252)
    SA_RS0612530S ribosomal protein S16  [2] (data from MRSA252)
    SA_RS0614050S ribosomal protein L19  [2] (data from MRSA252)
    SA_RS06165succinyl-CoA ligase subunit beta  [2] (data from MRSA252)
    SA_RS06170succinyl-CoA ligase subunit alpha  [2] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [2] (data from MRSA252)
    SA_RS06235elongation factor Ts  [2] (data from MRSA252)
    SA_RS06490glutamine synthetase  [2] (data from MRSA252)
    SA_RS06730aconitate hydratase  [2] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [2] (data from MRSA252)
    SA_RS07955molecular chaperone DnaK  [2] (data from MRSA252)
    SA_RS0828550S ribosomal protein L27  [2] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [2] (data from MRSA252)
    SA_RS08435trigger factor  [2] (data from MRSA252)
    SA_RS0846050S ribosomal protein L20  [2] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [2] (data from MRSA252)
    SA_RS08565ATP-dependent 6-phosphofructokinase  [2] (data from MRSA252)
    SA_RS08630acetate kinase  [2] (data from MRSA252)
    SA_RS0867530S ribosomal protein S4  [2] (data from MRSA252)
    SA_RS08760formate--tetrahydrofolate ligase  [2] (data from MRSA252)
    SA_RS09960manganese-dependent inorganic pyrophosphatase  [2] (data from MRSA252)
    SA_RS10540co-chaperone GroES  [2] (data from MRSA252)
    SA_RS1105050S ribosomal protein L31 type B  [2] (data from MRSA252)
    SA_RS11075fructose-bisphosphate aldolase  [2] (data from MRSA252)
    SA_RS11085CTP synthetase  [2] (data from MRSA252)
    SA_RS11245glutamine--fructose-6-phosphate aminotransferase  [2] (data from MRSA252)
    SA_RS11430Asp23/Gls24 family envelope stress response protein  [2] (data from MRSA252)
    SA_RS1160030S ribosomal protein S9  [2] (data from MRSA252)
    SA_RS1163050S ribosomal protein L17  [2] (data from MRSA252)
    SA_RS1164030S ribosomal protein S11  [2] (data from MRSA252)
    SA_RS1164530S ribosomal protein S13  [2] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [2] (data from MRSA252)
    SA_RS1168550S ribosomal protein L18  [2] (data from MRSA252)
    SA_RS1170550S ribosomal protein L5  [2] (data from MRSA252)
    SA_RS1171550S ribosomal protein L14  [2] (data from MRSA252)
    SA_RS1173530S ribosomal protein S3  [2] (data from MRSA252)
    SA_RS1174530S ribosomal protein S19  [2] (data from MRSA252)
    SA_RS1175050S ribosomal protein L2  [2] (data from MRSA252)
    SA_RS126452,3-bisphosphoglycerate-dependent phosphoglycerate mutase  [2] (data from MRSA252)
    SA_RS13255lactate dehydrogenase  [2] (data from MRSA252)
    SA_RS13420L-glutamate gamma-semialdehyde dehydrogenase  [2] (data from MRSA252)
    SA_RS13730class I fructose-bisphosphate aldolase  [2] (data from MRSA252)
    SA_RS13735malate:quinone oxidoreductase  [2] (data from MRSA252)
    SA_RS13920arginine deiminase  [2] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[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: 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]

  1. ↑ R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
    A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
    Mol Microbiol: 2002, 43(6);1387-400
    [PubMed:11952893] [WorldCat.org] [DOI] (P p)
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 2.29 2.30 2.31 2.32 2.33 2.34 2.35 2.36 2.37 2.38 2.39 2.40 2.41 2.42 2.43 2.44 2.45 2.46 2.47 2.48 2.49 2.50 2.51 2.52 2.53 2.54 2.55 2.56 2.57 2.58 2.59 2.60 2.61 2.62 2.63 2.64 2.65 2.66 2.67 2.68 2.69 2.70 2.71 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)

⊟Relevant publications[edit | edit source]

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