From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1274 [new locus tag: SACOL_RS06505 ]
  • pan locus tag?: SAUPAN003555000
  • symbol: rpsB
  • pan gene symbol?: rpsB
  • synonym:
  • product: 30S ribosomal protein S2

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1274 [new locus tag: SACOL_RS06505 ]
  • symbol: rpsB
  • product: 30S ribosomal protein S2
  • replicon: chromosome
  • strand: +
  • coordinates: 1284586..>1285350
  • length: 765
  • 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
    421
    481
    541
    601
    661
    721
    ATGGCAGTAATTTCAATGAAACAATTACTAGAAGCGGGTGTTCACTTCGGTCACCAAACA
    CGTCGTTGGAACCCAAAAATGAAAAAATATATCTTCACTGAGAGAAATGGTATTTATATC
    ATCGACTTACAAAAAACAGTGAAAAAAGTAGACGAGGCATACAACTTCTTGAAACAAGTT
    TCAGAAGATGGTGGACAAGTCTTATTCGTAGGAACTAAAAAACAAGCACAAGAATCAGTT
    AAATCTGAAGCAGAACGTGCTGGTCAATTCTACATTAACCAAAGATGGTTAGGTGGATTA
    TTAACTAACTATAAAACGATCTCAAAACGAATCAAACGTATTTCTGAAATTGAAAAAATG
    GAAGAAGATGGTTTATTCGAAGTATTACCTAAAAAAGAAGTAGTAGAACTTAAAAAAGAA
    TACGACCGTTTAATCAAATTCTTAGGCGGAATTCGTGATATGAAATCAATGCCTCAAGCA
    TTATTCGTAGTTGACCCACGTAAAGAGCGTAATGCAATTGCTGAAGCTCGTAAATTAAAT
    ATTCCTATCGTAGGTATCGTTGACACTAACTGTGATCCTGACGAAATTGACTACGTTATC
    CCAGCAAACGACGATGCTATCCGTGCGGTTAAATTATTAACTGCTAAAATGGCAGATGCA
    ATCTTAGAAGGTCAACAAGGCGTTTCTAATGAAGAAGTAGCTGCAGAACAAAACATCGAT
    TTAGATGAAAAAGAAAAATCAGAAGAAACAGAAGCAACAGAAGCA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    765

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1274 [new locus tag: SACOL_RS06505 ]
  • symbol: RpsB
  • description: 30S ribosomal protein S2
  • length: 255
  • theoretical pI: 5.33411
  • theoretical MW: 29036.1
  • GRAVY: -0.50902

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS2 (TIGR01011; HMM-score: 365.1)
    and 1 more
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS2 (TIGR01012; HMM-score: 97.3)
  • TheSEED  :
    • SSU ribosomal protein S2p (SAe)
    Protein Metabolism Protein biosynthesis Ribosome SSU bacterial  SSU ribosomal protein S2p (SAe)
  • PFAM:
    SIS (CL0067) Ribosomal_S2; Ribosomal protein S2 (PF00318; HMM-score: 333.9)

⊟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): 0.001567
    • TAT(Tat/SPI): 0.000142
    • LIPO(Sec/SPII): 0.000329
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAVISMKQLLEAGVHFGHQTRRWNPKMKKYIFTERNGIYIIDLQKTVKKVDEAYNFLKQVSEDGGQVLFVGTKKQAQESVKSEAERAGQFYINQRWLGGLLTNYKTISKRIKRISEIEKMEEDGLFEVLPKKEVVELKKEYDRLIKFLGGIRDMKSMPQALFVVDPRKERNAIAEARKLNIPIVGIVDTNCDPDEIDYVIPANDDAIRAVKLLTAKMADAILEGQQGVSNEEVAAEQNIDLDEKEKSEETEATEA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 4285 [5]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [6] (data from MRSA252)
    SACOL1385(acnA)aconitate hydratase  [6] (data from MRSA252)
    SACOL0660(adhP)alcohol dehydrogenase  [6] (data from MRSA252)
    SACOL2218(adk)adenylate kinase  [6] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [6] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL2656(arcB2)ornithine carbamoyltransferase  [6] (data from MRSA252)
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1215(carB)carbamoyl phosphate synthase large subunit  [6] (data from MRSA252)
    SACOL1721(clpX)ATP-dependent protease ATP-binding subunit ClpX  [6] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [6] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL0937(dltC)D-alanine--poly(phosphoribitol) ligase subunit 2  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0002(dnaN)DNA polymerase III subunit beta  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [6] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [6] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [6] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [6] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [6] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [6] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [6] (data from MRSA252)
    SACOL1622(glyS)glycyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1554(gnd)6-phosphogluconate dehydrogenase  [6] (data from MRSA252)
    SACOL2415(gpmA)phosphoglyceromutase  [6] (data from MRSA252)
    SACOL2017(groES)co-chaperonin GroES  [6] (data from MRSA252)
    SACOL1638(grpE)heat shock protein GrpE  [6] (data from MRSA252)
    SACOL0461(guaA)GMP synthase  [6] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [6] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [6] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL0562(lysS)lysyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1054(menB)naphthoate synthase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL2615(panB)3-methyl-2-oxobutanoate hydroxymethyltransferase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1746(pfkA)6-phosphofructokinase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [6] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0015(rplI)50S ribosomal protein L9  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL2228(rplX)50S ribosomal protein L24  [6] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [6] (data from MRSA252)
    SACOL1700(rpmA)50S ribosomal protein L27  [6] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [6] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [6] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [6] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [6] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL1254(rpsP)30S ribosomal protein S16  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL0009(serS)seryl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1610(sodA2)superoxide dismutase  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [6] (data from MRSA252)
    SACOL1263(sucD)succinyl-CoA synthetase subunit alpha  [6] (data from MRSA252)
    SACOL1722(tig)trigger factor  [6] (data from MRSA252)
    SACOL1377(tkt)transketolase  [6] (data from MRSA252)
    SACOL0840(tpiA)triosephosphate isomerase  [6] (data from MRSA252)
    SACOL1155(trxA)thioredoxin  [6] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0435GTP-dependent nucleic acid-binding protein EngD  [6] (data from MRSA252)
    SACOL0444hypothetical protein  [6] (data from MRSA252)
    SACOL0457hypothetical protein  [6] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [6] (data from MRSA252)
    SACOL0688ABC transporter substrate-binding protein  [6] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL1952ferritins family protein  [6] (data from MRSA252)
    SACOL2163hypothetical protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)
    SACOL2535D-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [6] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [6] (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: 17.99 h [7]

⊟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. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ 6.000 6.001 6.002 6.003 6.004 6.005 6.006 6.007 6.008 6.009 6.010 6.011 6.012 6.013 6.014 6.015 6.016 6.017 6.018 6.019 6.020 6.021 6.022 6.023 6.024 6.025 6.026 6.027 6.028 6.029 6.030 6.031 6.032 6.033 6.034 6.035 6.036 6.037 6.038 6.039 6.040 6.041 6.042 6.043 6.044 6.045 6.046 6.047 6.048 6.049 6.050 6.051 6.052 6.053 6.054 6.055 6.056 6.057 6.058 6.059 6.060 6.061 6.062 6.063 6.064 6.065 6.066 6.067 6.068 6.069 6.070 6.071 6.072 6.073 6.074 6.075 6.076 6.077 6.078 6.079 6.080 6.081 6.082 6.083 6.084 6.085 6.086 6.087 6.088 6.089 6.090 6.091 6.092 6.093 6.094 6.095 6.096 6.097 6.098 6.099 6.100 6.101 6.102 6.103 6.104 6.105 6.106 6.107 6.108 6.109 6.110 6.111 6.112 6.113 6.114 6.115 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)
  7. ↑ 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]

Retrieved from "http://aureowiki.med.uni-greifswald.de/index.php?title=SACOL1274&oldid=83000"