From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0003 [new locus tag: SACOL_RS00035 ]
  • pan locus tag?: SAUPAN000009000
  • symbol: SACOL0003
  • pan gene symbol?: —
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0003 [new locus tag: SACOL_RS00035 ]
  • symbol: SACOL0003
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 3697..3942
  • length: 246
  • 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
    GTGATTATTTTGGTTCAAGAAGTTGTAGTAGAAGGAGACATTAATTTAGGTCAATTTCTA
    AAAACAGAAGGGATTATTGAATCTGGTGGTCAAGCAAAATGGTTCTTGCAAGACGTTGAA
    GTATTAATTAATGGAGTGCGTGAAACACGTCGCGGTAAAAAGTTAGAACATCAAGATCGT
    ATAGATATCCCAGAATTACCTGAAGATGCTGGTTCTTTCTTAATCATTCATCAAGGTGAA
    CAATGA
    60
    120
    180
    240
    246

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0003 [new locus tag: SACOL_RS00035 ]
  • symbol: SACOL0003
  • description: hypothetical protein
  • length: 81
  • theoretical pI: 4.35578
  • theoretical MW: 9137.35
  • GRAVY: -0.197531

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing DNA metabolism DNA replication, recombination, and repair S4 domain protein YaaA (TIGR02988; HMM-score: 90)
  • TheSEED  :
    • FIG002958: hypothetical protein
    Hypothetical Coupled to RecF  FIG002958: hypothetical protein
  • PFAM:
    S4 (CL0492) S4_2; S4 domain (PF13275; HMM-score: 74.4)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • 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): 0.002067
    • TAT(Tat/SPI): 0.000157
    • LIPO(Sec/SPII): 0.000268
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MIILVQEVVVEGDINLGQFLKTEGIIESGGQAKWFLQDVEVLINGVRETRRGKKLEHQDRIDIPELPEDAGSFLIIHQGEQ

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 3920 [4]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL0660(adhP)alcohol dehydrogenase  [5] (data from MRSA252)
    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)
    SACOL1685(aspS)aspartyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL0570(clpC)  [5] (data from MRSA252)
    SACOL2074(ddl)D-alanyl-alanine synthetase A  [5] (data from MRSA252)
    SACOL0123(deoC1)deoxyribose-phosphate aldolase  [5] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL1587(efp)elongation factor P  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0634(eutD)phosphotransacetylase  [5] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [5] (data from MRSA252)
    SACOL2091(fabZ)(3R)-hydroxymyristoyl-ACP dehydratase  [5] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL1410(femA)femA protein  [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)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [5] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [5] (data from MRSA252)
    SACOL1742(gltA)citrate synthase  [5] (data from MRSA252)
    SACOL0574(gltX)glutamyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [5] (data from MRSA252)
    SACOL1622(glyS)glycyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1554(gnd)6-phosphogluconate dehydrogenase  [5] (data from MRSA252)
    SACOL2415(gpmA)phosphoglyceromutase  [5] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1206(ileS)isoleucyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL0240(ispD)2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase  [5] (data from MRSA252)
    SACOL1368(kataA)catalase  [5] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL0562(lysS)lysyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL0746(norR)MarR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0793(nrdF)ribonucleotide-diphosphate reductase subunit beta  [5] (data from MRSA252)
    SACOL0582(nusG)transcription antitermination protein  [5] (data from MRSA252)
    SACOL1838(pckA)phosphoenolpyruvate carboxykinase  [5] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [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)
    SACOL0841(pgm)phosphoglyceromutase  [5] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [5] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [5] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [5] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [5] (data from MRSA252)
    SACOL1610(sodA2)superoxide dismutase  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [5] (data from MRSA252)
    SACOL1831(tal)translaldolase  [5] (data from MRSA252)
    SACOL0840(tpiA)triosephosphate isomerase  [5] (data from MRSA252)
    SACOL1762(tpx)thiol peroxidase  [5] (data from MRSA252)
    SACOL1155(trxA)thioredoxin  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL0426acetyl-CoA acetyltransferase  [5] (data from MRSA252)
    SACOL0521hypothetical protein  [5] (data from MRSA252)
    SACOL0707dihydroxyacetone kinase subunit DhaK  [5] (data from MRSA252)
    SACOL0721hypothetical protein  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0742hypothetical protein  [5] (data from MRSA252)
    SACOL0876hypothetical protein  [5] (data from MRSA252)
    SACOL1020hypothetical protein  [5] (data from MRSA252)
    SACOL1099hypothetical protein  [5] (data from MRSA252)
    SACOL1437CSD family cold shock protein  [5] (data from MRSA252)
    SACOL1593glycine dehydrogenase subunit 2  [5] (data from MRSA252)
    SACOL1801dipeptidase PepV  [5] (data from MRSA252)
    SACOL1946methionine aminopeptidase  [5] (data from MRSA252)
    SACOL2131Dps family protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)
    SACOL2296glycerate dehydrogenase  [5] (data from MRSA252)
    SACOL2535D-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [5] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [5] (data from MRSA252)
    SACOL2609hypothetical protein  [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: no data available

⊟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 5.56 5.57 5.58 5.59 5.60 5.61 5.62 5.63 5.64 5.65 5.66 5.67 5.68 5.69 5.70 5.71 5.72 5.73 5.74 5.75 5.76 5.77 5.78 5.79 5.80 5.81 5.82 5.83 5.84 5.85 5.86 5.87 5.88 5.89 5.90 5.91 5.92 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 | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL0003&oldid=92593"