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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0586 [new locus tag: SACOL_RS03040 ]
  • pan locus tag?: SAUPAN002311000
  • symbol: rplL
  • pan gene symbol?: rplL
  • synonym:
  • product: 50S ribosomal protein L7/L12

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0586 [new locus tag: SACOL_RS03040 ]
  • symbol: rplL
  • product: 50S ribosomal protein L7/L12
  • replicon: chromosome
  • strand: +
  • coordinates: 605622..605990
  • length: 369
  • 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
    ATGGCTAATCATGAACAAATCATTGAAGCGATTAAAGAAATGTCAGTATTAGAATTAAAC
    GACTTAGTAAAAGCAATTGAAGAAGAATTTGGTGTAACTGCAGCTGCTCCAGTAGCAGTA
    GCAGGTGCAGCTGGTGGCGCTGACGCTGCAGCAGAAAAAACTGAATTTGACGTTGAGTTA
    ACTTCAGCTGGTTCATCTAAAATCAAAGTTGTTAAAGCTGTTAAAGAAGCAACTGGTTTA
    GGATTAAAAGATGCTAAAGAATTAGTAGACGGAGCTCCTAAAGTAATCAAAGAAGCTTTA
    CCTAAAGAAGAAGCTGAAAAACTTAAAGAACAATTAGAAGAAGTTGGAGCTACTGTAGAA
    TTAAAATAA
    60
    120
    180
    240
    300
    360
    369

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0586 [new locus tag: SACOL_RS03040 ]
  • symbol: RplL
  • description: 50S ribosomal protein L7/L12
  • length: 122
  • theoretical pI: 4.32374
  • theoretical MW: 12711.5
  • GRAVY: -0.0483607

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bL12 (TIGR00855; HMM-score: 158.6)
  • TheSEED  :
    • LSU ribosomal protein L7p/L12p (P1/P2)
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L7/L12 (P1/P2)
  • PFAM:
    no clan defined Ribosomal_L12; Ribosomal protein L7/L12 C-terminal domain (PF00542; HMM-score: 103.3)
    and 6 more
    Ribosomal_L12_N; Ribosomal protein L7/L12 dimerisation domain (PF16320; HMM-score: 75.9)
    IHF-likeDNA-bdg (CL0548) Bac_DNA_binding; Bacterial DNA-binding protein (PF00216; HMM-score: 15.3)
    no clan defined DUF2267; Uncharacterized conserved protein (DUF2267) (PF10025; HMM-score: 14.2)
    PP2C_C; Protein serine/threonine phosphatase 2C, C-terminal domain (PF07830; HMM-score: 13.3)
    PTS_IIA; PTS system, Lactose/Cellobiose specific IIA subunit (PF02255; HMM-score: 12.5)
    HTH (CL0123) HTH_33; Winged helix-turn helix (PF13592; HMM-score: 11.8)

⊟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: 0.67
    • Signal peptide possibility: -0.5
    • N-terminally Anchored Score: -2
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.057639
    • TAT(Tat/SPI): 0.076736
    • LIPO(Sec/SPII): 0.001562
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MANHEQIIEAIKEMSVLELNDLVKAIEEEFGVTAAAPVAVAGAAGGADAAAEKTEFDVELTSAGSSKIKVVKAVKEATGLGLKDAKELVDGAPKVIKEALPKEEAEKLKEQLEEVGATVELK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4] [5]
  • quantitative data / protein copy number per cell: 8346 [6]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [7] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [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)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [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)
    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)
    SACOL2618(ldh2)L-lactate dehydrogenase  [7] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [7] (data from MRSA252)
    SACOL0746(norR)MarR family transcriptional regulator  [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)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [7] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [7] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [7] (data from MRSA252)
    SACOL1293(pnp)polynucleotide phosphorylase/polyadenylase  [7] (data from MRSA252)
    SACOL1092(ptsI)phosphoenolpyruvate-protein phosphotransferase  [7] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [7] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [7] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [7] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [7] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [7] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [7] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [7] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [7] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [7] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [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)
    SACOL2234(rplV)50S ribosomal protein L22  [7] (data from MRSA252)
    SACOL2221(rpmD)50S ribosomal protein L30  [7] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [7] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [7] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [7] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [7] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [7] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [7] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [7] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [7] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [7] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [7] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [7] (data from MRSA252)
    SACOL0816(secA)preprotein translocase subunit SecA  [7] (data from MRSA252)
    SACOL1610(sodA2)superoxide dismutase  [7] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [7] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [7] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [7] (data from MRSA252)
    SACOL1831(tal)translaldolase  [7] (data from MRSA252)
    SACOL1377(tkt)transketolase  [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)
    SACOL03035'-nucleotidase  [7] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [7] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [7] (data from MRSA252)
    SACOL1437CSD family cold shock protein  [7] (data from MRSA252)
    SACOL1753universal stress protein  [7] (data from MRSA252)
    SACOL1759universal stress protein  [7] (data from MRSA252)
    SACOL1836hypothetical protein  [7] (data from MRSA252)
    SACOL1952ferritins family protein  [7] (data from MRSA252)
    SACOL1973hypothetical protein  [7] (data from MRSA252)
    SACOL2163hypothetical protein  [7] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [7] (data from MRSA252)
    SACOL2266molybdopterin biosynthesis MoeA protein  [7] (data from MRSA252)
    SACOL2469glutamate synthase  [7] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [7] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: L10 leader (transcription termination) regulon
    L10 leader(RNA)important in Ribosome biogenesis; transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 19.63 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 7.72 7.73 7.74 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]

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