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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2225 [new locus tag: SACOL_RS11710 ]
  • pan locus tag?: SAUPAN005688000
  • symbol: rpsH
  • pan gene symbol?: rpsH
  • synonym:
  • product: 30S ribosomal protein S8

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2225 [new locus tag: SACOL_RS11710 ]
  • symbol: rpsH
  • product: 30S ribosomal protein S8
  • replicon: chromosome
  • strand: -
  • coordinates: 2300413..2300811
  • length: 399
  • 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
    ATGACAATGACAGATCCAATCGCAGATATGCTTACTCGTGTAAGAAACGCAAACATGGTG
    CGTCACGAGAAGTTAGAATTACCTGCATCAAATATTAAAAAAGAAATTGCTGAAATCTTA
    AAGAGTGAAGGTTTCATTAAAAATGTTGAATACGTAGAAGATGATAAACAAGGTGTACTT
    CGTTTATTCTTAAAATATGGTCAAAACGATGAGCGTGTTATCACAGGATTAAAACGTATT
    TCAAAACCAGGTTTACGTGTTTATGCAAAAGCTAGCGAAATGCCTAAAGTATTAAATGGT
    TTAGGTATTGCATTAGTATCAACTTCTGAAGGTGTAATCACTGACAAAGAAGCAAGAAAA
    CGTAATGTTGGTGGAGAAATTATCGCATACGTTTGGTAA
    60
    120
    180
    240
    300
    360
    399

⊟Protein[edit | edit source]

Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5TCU

⊟General[edit | edit source]

  • locus tag: SACOL2225 [new locus tag: SACOL_RS11710 ]
  • symbol: RpsH
  • description: 30S ribosomal protein S8
  • length: 132
  • theoretical pI: 9.90457
  • theoretical MW: 14831.2
  • GRAVY: -0.284848

⊟Function[edit | edit source]

  • TIGRFAM:
    integral membrane protein (TIGR04561; HMM-score: 14.3)
    Unknown function General zinc finger protein ZPR1 homolog (TIGR00340; HMM-score: 12.5)
  • TheSEED  :
    • SSU ribosomal protein S8p (S15Ae)
    Protein Metabolism Protein biosynthesis Ribosome SSU bacterial  SSU ribosomal protein S8p (S15Ae)
  • PFAM:
    no clan defined Ribosomal_S8; Ribosomal protein S8 (PF00410; HMM-score: 180.8)

⊟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: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.004597
    • TAT(Tat/SPI): 0.000216
    • LIPO(Sec/SPII): 0.000697
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTMTDPIADMLTRVRNANMVRHEKLELPASNIKKEIAEILKSEGFIKNVEYVEDDKQGVLRLFLKYGQNDERVITGLKRISKPGLRVYAKASEMPKVLNGLGIALVSTSEGVITDKEARKRNVGGEIIAYVW

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 4005 [4]
  • interaction partners:
    SACOL2218(adk)adenylate kinase  [5] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [5] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL2656(arcB2)ornithine carbamoyltransferase  [5] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0634(eutD)phosphotransacetylase  [5] (data from MRSA252)
    SACOL0988(fabF)3-oxoacyl-ACP synthase  [5] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [5] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [5] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [5] (data from MRSA252)
    SACOL1622(glyS)glycyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1206(ileS)isoleucyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL1285(nusA)transcription elongation factor NusA  [5] (data from MRSA252)
    SACOL1005(pepF)oligoendopeptidase F  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [5] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [5] (data from MRSA252)
    SACOL1982(ppaC)manganese-dependent inorganic pyrophosphatase  [5] (data from MRSA252)
    SACOL1092(ptsI)phosphoenolpyruvate-protein phosphotransferase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [5] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SACOL1263(sucD)succinyl-CoA synthetase subunit alpha  [5] (data from MRSA252)
    SACOL1831(tal)translaldolase  [5] (data from MRSA252)
    SACOL1722(tig)trigger factor  [5] (data from MRSA252)
    SACOL1155(trxA)thioredoxin  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0521hypothetical protein  [5] (data from MRSA252)
    SACOL0721hypothetical protein  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0876hypothetical protein  [5] (data from MRSA252)
    SACOL0975coenzyme A disulfide reductase  [5] (data from MRSA252)
    SACOL1020hypothetical protein  [5] (data from MRSA252)
    SACOL1099hypothetical protein  [5] (data from MRSA252)
    SACOL1588proline dipeptidase  [5] (data from MRSA252)
    SACOL1946methionine aminopeptidase  [5] (data from MRSA252)
    SACOL2296glycerate dehydrogenase  [5] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [5] (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: 8.32 h [6]

⊟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, 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 5.51 5.52 5.53 5.54 5.55 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)
  6. ↑ 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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