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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2237 [new locus tag: SACOL_RS11770 ]
  • pan locus tag?: SAUPAN005700000
  • symbol: rplW
  • pan gene symbol?: rplW
  • synonym:
  • product: 50S ribosomal protein L23

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2237 [new locus tag: SACOL_RS11770 ]
  • symbol: rplW
  • product: 50S ribosomal protein L23
  • replicon: chromosome
  • strand: -
  • coordinates: 2305563..2305838
  • length: 276
  • 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
    ATGGAAGCAAGAGATATTCTTAAGCGCCCCGTAATCACTGAGAAATCTTCTGAAGCAATG
    GCTGAAGACAAATACACTTTCGACGTTGATACTCGTGTTAACAAAACACAAGTAAAAATG
    GCAGTTGAAGAAATCTTCAACGTAAAAGTTGCAAGTGTTAATATCATGAATTACAAACCT
    AAGAAAAAACGTATGGGCCGTTACCAAGGCTATACAAACAAAAGAAGAAAAGCGATTGTA
    ACTCTTAAAGAAGGATCAATCGACTTATTTAACTAA
    60
    120
    180
    240
    276

⊟Protein[edit | edit source]

Protein Data Bank: 4WCE
Protein Data Bank: 4WF9
Protein Data Bank: 4WFA
Protein Data Bank: 4WFB
Protein Data Bank: 5HKV
Protein Data Bank: 5HL7
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5NRG
Protein Data Bank: 5TCU

⊟General[edit | edit source]

  • locus tag: SACOL2237 [new locus tag: SACOL_RS11770 ]
  • symbol: RplW
  • description: 50S ribosomal protein L23
  • length: 91
  • theoretical pI: 10.4702
  • theoretical MW: 10605.3
  • GRAVY: -0.706593

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL23 (TIGR03636; HMM-score: 36.8)
  • TheSEED  :
    • LSU ribosomal protein L23p (L23Ae)
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L23p (L23Ae)
  • PFAM:
    no clan defined Ribosomal_L23; Ribosomal protein L23 (PF00276; HMM-score: 110.3)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.012683
    • TAT(Tat/SPI): 0.000806
    • LIPO(Sec/SPII): 0.001254
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MEARDILKRPVITEKSSEAMAEDKYTFDVDTRVNKTQVKMAVEEIFNVKVASVNIMNYKPKKKRMGRYQGYTNKRRKAIVTLKEGSIDLFN

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4] [5]
  • quantitative data / protein copy number per cell: 3190 [6]
  • interaction partners:
    SACOL0833(clpP)ATP-dependent Clp protease proteolytic subunit  [7] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [7] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [7] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [7] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [7] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [7] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [7] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [7] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [7] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [7] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [7] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [7] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [7] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [7] (data from MRSA252)
    SACOL1206(ileS)isoleucyl-tRNA synthetase  [7] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [7] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [7] (data from MRSA252)
    SACOL0240(ispD)2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase  [7] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [7] (data from MRSA252)
    SACOL1285(nusA)transcription elongation factor NusA  [7] (data from MRSA252)
    SACOL1838(pckA)phosphoenolpyruvate carboxykinase  [7] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [7] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [7] (data from MRSA252)
    SACOL1005(pepF)oligoendopeptidase F  [7] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [7] (data from MRSA252)
    SACOL1982(ppaC)manganese-dependent inorganic pyrophosphatase  [7] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [7] (data from MRSA252)
    SACOL1092(ptsI)phosphoenolpyruvate-protein phosphotransferase  [7] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [7] (data from MRSA252)
    SACOL1213(pyrC)dihydroorotase  [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)
    SACOL2227(rplE)50S ribosomal protein L5  [7] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [7] (data from MRSA252)
    SACOL0015(rplI)50S ribosomal protein L9  [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)
    SACOL2220(rplO)50S ribosomal protein L15  [7] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [7] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [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)
    SACOL2228(rplX)50S ribosomal protein L24  [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)
    SACOL1516(rpsA)30S ribosomal protein S1  [7] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [7] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [7] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [7] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [7] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [7] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [7] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [7] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [7] (data from MRSA252)
    SACOL1642(rpsT)30S ribosomal protein S20  [7] (data from MRSA252)
    SACOL1722(tig)trigger factor  [7] (data from MRSA252)
    SACOL1377(tkt)transketolase  [7] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [7] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [7] (data from MRSA252)
    SACOL03035'-nucleotidase  [7] (data from MRSA252)
    SACOL0521hypothetical protein  [7] (data from MRSA252)
    SACOL0599hypothetical protein  [7] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [7] (data from MRSA252)
    SACOL0876hypothetical protein  [7] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [7] (data from MRSA252)
    SACOL1593glycine dehydrogenase subunit 2  [7] (data from MRSA252)
    SACOL1615DEAD/DEAH box helicase  [7] (data from MRSA252)
    SACOL1670hypothetical protein  [7] (data from MRSA252)
    SACOL1753universal stress protein  [7] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [7] (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: 11.26 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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