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NCBI: 26-AUG-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus N315
  • locus tag: SA0498 [new locus tag: SA_RS02920 ]
  • pan locus tag?: SAUPAN002311000
  • symbol: rplL
  • pan gene symbol?: rplL
  • synonym:
  • product: 50S ribosomal protein L7/L12

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SA0498 [new locus tag: SA_RS02920 ]
  • symbol: rplL
  • product: 50S ribosomal protein L7/L12
  • replicon: chromosome
  • strand: +
  • coordinates: 578254..578622
  • length: 369
  • essential: yes [1] DEG other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 1
    61
    121
    181
    241
    301
    361
    ATGGCTAATCATGAACAAATCATTGAAGCGATTAAAGAAATGTCAGTATTAGAATTAAAC
    GACTTAGTAAAAGCAATTGAAGAAGAATTTGGTGTAACTGCAGCTGCTCCAGTAGCAGTA
    GCAGGTGCAGCTGGTGGCGCTGACGCTGCAGCAGAAAAAACTGAATTTGACGTTGAGTTA
    ACTTCAGCTGGTTCATCTAAAATCAAAGTTGTTAAAGCTGTTAAAGAAGCAACTGGTTTA
    GGATTAAAAGATGCTAAAGAATTAGTAGACGGAGCTCCTAAAGTAATCAAAGAAGCTTTA
    CCTAAAGAAGAAGCTGAAAAACTTAAAGAACAATTAGAAGAAGTTGGAGCTACTGTAGAA
    TTAAAATAA
    60
    120
    180
    240
    300
    360
    369

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SA0498 [new locus tag: SA_RS02920 ]
  • symbol: RplL
  • description: 50S ribosomal protein L7/L12
  • length: 122
  • theoretical pI: 4.32374
  • theoretical MW: 12711.5
  • GRAVY: -0.0483607

Function[edit source | edit]

  • reaction:
  • TIGRFAM:
    Genetic information processingProtein synthesisRibosomal proteins: synthesis and modificationribosomal protein bL12 (TIGR00855; HMM-score: 158.6)
  • TheSEED:  
    Ribosome LSU bacterial LSU ribosomal protein L7p/L12p (P1/P2) 
  • PFAM:
    no clan definedRibosomal_L12; Ribosomal protein L7/L12 C-terminal domain (PF00542; HMM-score: 103.3)
    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 definedDUF2267; 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 & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SA1533(ackA)acetate kinase  [2] (data from MRSA252)
    SA0366(ahpC)alkyl hydroperoxide reductase  [2] (data from MRSA252)
    SA1984(asp23)alkaline shock protein 23  [2] (data from MRSA252)
    SA1517(citC)isocitrate dehydrogenase  [2] (data from MRSA252)
    SA1234(cspA)cold-shock protein CspA  [2] (data from MRSA252)
    SA0471(cysK)hypothetical protein  [2] (data from MRSA252)
    SA1409(dnaK)molecular chaperone DnaK  [2] (data from MRSA252)
    SA0731(eno)phosphopyruvate hydratase  [2] (data from MRSA252)
    SA1029(ftsZ)cell division protein FtsZ  [2] (data from MRSA252)
    SA0505(fus)elongation factor G  [2] (data from MRSA252)
    SA0727(gap)glyceraldehyde-3-phosphate dehydrogenase  [2] (data from MRSA252)
    SA0375(guaB)inositol-monophosphate dehydrogenase  [2] (data from MRSA252)
    SA1305(hu)DNA-binding protein II  [2] (data from MRSA252)
    SA2068(moeA)molybdopterin biosynthesis protein moeA  [2] (data from MRSA252)
    SA2400(mqo2)malate:quinone oxidoreductase  [2] (data from MRSA252)
    SA1244(odhB)dihydrolipoamide succinyltransferase  [2] (data from MRSA252)
    SA0943-1(pdhA)pyruvate dehydrogenase E1 component subunit alpha  [2] (data from MRSA252)
    SA0944(pdhB)pyruvate dehydrogenase E1 component subunit beta  [2] (data from MRSA252)
    SA0945(pdhC)branched-chain alpha-keto acid dehydrogenase E2 subunit  [2] (data from MRSA252)
    SA0946(pdhD)dihydrolipoamide dehydrogenase  [2] (data from MRSA252)
    SA1938(pdp)pyrimidine-nucleoside phosphorylase  [2] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [2] (data from MRSA252)
    SA0728(pgk)phosphoglycerate kinase  [2] (data from MRSA252)
    SA1117(pnpA)polynucleotide phosphorylase  [2] (data from MRSA252)
    SA0935(ptsI)phosphoenolpyruvate-protein phosphatase  [2] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [2] (data from MRSA252)
    SA2341(rocA)1-pyrroline-5-carboxylate dehydrogenase  [2] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [2] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [2] (data from MRSA252)
    SA2047(rplC)50S ribosomal protein L3  [2] (data from MRSA252)
    SA2046(rplD)50S ribosomal protein L4  [2] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [2] (data from MRSA252)
    SA0497(rplJ)50S ribosomal protein L10  [2] (data from MRSA252)
    SA0495(rplK)50S ribosomal protein L11  [2] (data from MRSA252)
    SA2017(rplM)50S ribosomal protein L13  [2] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [2] (data from MRSA252)
    SA2032(rplR)50S ribosomal protein L18  [2] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [2] (data from MRSA252)
    SA1502(rplT)50S ribosomal protein L20  [2] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [2] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [2] (data from MRSA252)
    SA2030(rpmD)50S ribosomal protein L30  [2] (data from MRSA252)
    SA0500(rpoB)DNA-directed RNA polymerase subunit beta  [2] (data from MRSA252)
    SA1308(rpsA)30S ribosomal protein S1  [2] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [2] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [2] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [2] (data from MRSA252)
    SA0352(rpsF)30S ribosomal protein S6  [2] (data from MRSA252)
    SA0504(rpsG)30S ribosomal protein S7  [2] (data from MRSA252)
    SA2016(rpsI)30S ribosomal protein S9  [2] (data from MRSA252)
    SA2024(rpsK)30S ribosomal protein S11  [2] (data from MRSA252)
    SA0503(rpsL)30S ribosomal protein S12  [2] (data from MRSA252)
    SA2025(rpsM)30S ribosomal protein S13  [2] (data from MRSA252)
    SA0708(secA)preprotein translocase subunit SecA  [2] (data from MRSA252)
    SA1382(sodA)superoxide dismutase SodA  [2] (data from MRSA252)
    SA0107(spa)immunoglobulin G binding protein A  [2] (data from MRSA252)
    SA1245(sucA)2-oxoglutarate dehydrogenase E1  [2] (data from MRSA252)
    SA1177(tkt)transketolase  [2] (data from MRSA252)
    SA0729(tpiA)triosephosphate isomerase  [2] (data from MRSA252)
    SA1100(tsf)elongation factor Ts  [2] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [2] (data from MRSA252)
    SA0295hypothetical protein  [2] (data from MRSA252)
    SA0641hypothetical protein  [2] (data from MRSA252)
    SA0802hypothetical protein  [2] (data from MRSA252)
    SA0829hypothetical protein  [2] (data from MRSA252)
    SA1528hypothetical protein  [2] (data from MRSA252)
    SA1532hypothetical protein  [2] (data from MRSA252)
    SA1599translaldolase  [2] (data from MRSA252)
    SA1607hypothetical protein  [2] (data from MRSA252)
    SA1709hypothetical protein  [2] (data from MRSA252)
    SA1727hypothetical protein  [2] (data from MRSA252)
    SA2248hypothetical protein  [2] (data from MRSA252)
    SA2395L-lactate dehydrogenase  [2] (data from MRSA252)
    SA2399fructose-1,6-bisphosphate aldolase  [2] (data from MRSA252)
    SAS074hypothetical protein  [2] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.195
    • Ymax_pos: 50
    • Cmax: 0.243
    • Cmax_pos: 50
    • Smax: 0.389
    • Smax_pos: 49
    • Smean: 0.108
    • D: 0.161
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MANHEQIIEAIKEMSVLELNDLVKAIEEEFGVTAAAPVAVAGAAGGADAAAEKTEFDVELTSAGSSKIKVVKAVKEATGLGLKDAKELVDGAPKVIKEALPKEEAEKLKEQLEEVGATVELK

Experimental data[edit source | edit]

  • experimentally validated: no data available

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator: L10_leader
    L10_leader (RNA) important in Ribosome biogenesisRegPrecise

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  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] (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 2.72 2.73 2.74 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)

Relevant publications[edit source | edit]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J. Microbiol. Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)