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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2217 [new locus tag: SACOL_RS11670 ]
  • pan locus tag?: SAUPAN005680000
  • symbol: infA
  • pan gene symbol?: infA
  • synonym:
  • product: translation initiation factor IF-1

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2217 [new locus tag: SACOL_RS11670 ]
  • symbol: infA
  • product: translation initiation factor IF-1
  • replicon: chromosome
  • strand: -
  • coordinates: 2295921..2296139
  • length: 219
  • 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
    ATGGCTAAACAAGATGTAATTGAATTAGAAGGTACTGTATTAGATACTTTACCGAACGCA
    ATGTTTAAAGTAGAATTAGAAAATGGTCATGAGATTTTAGCTCACGTAAGTGGTAAAATC
    AGAATGAATTACATTCGTATTCTACCTGGCGACAAAGTAACTGTTGAGATGTCTCCGTAC
    GATTTAACACGCGGAAGAATTACTTATCGTTATAAATAA
    60
    120
    180
    219

⊟Protein[edit | edit source]

Protein Data Bank: 2N8N

⊟General[edit | edit source]

  • locus tag: SACOL2217 [new locus tag: SACOL_RS11670 ]
  • symbol: InfA
  • description: translation initiation factor IF-1
  • length: 72
  • theoretical pI: 7.67987
  • theoretical MW: 8279.59
  • GRAVY: -0.276389

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Translation factors translation initiation factor IF-1 (TIGR00008; HMM-score: 132.5)
    and 1 more
    Genetic information processing Protein synthesis Translation factors translation initiation factor eIF-1A (TIGR00523; HMM-score: 22)
  • TheSEED  :
    • Translation initiation factor 1
    Protein Metabolism Protein biosynthesis Translation initiation factors bacterial  Translation initiation factor 1
  • PFAM:
    OB (CL0021) eIF-1a; Translation initiation factor 1A / IF-1 (PF01176; HMM-score: 99.2)
    and 2 more
    RsgA_N; RsgA N-terminal domain (PF16745; HMM-score: 14.2)
    TOBE_2; TOBE domain (PF08402; HMM-score: 12.5)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 10
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0
    • Extracellular Score: 0
    • 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): 0.003057
    • TAT(Tat/SPI): 0.000252
    • LIPO(Sec/SPII): 0.000283
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKQDVIELEGTVLDTLPNAMFKVELENGHEILAHVSGKIRMNYIRILPGDKVTVEMSPYDLTRGRITYRYK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2]
  • quantitative data / protein copy number per cell: 1179 [3]
  • interaction partners:
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [4] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [4] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [4] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [4] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [4] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [4] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [4] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [4] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [4] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [4] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [4] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [4] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [4] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [4] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [4] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [4] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [4] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [4] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [4] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [4] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [4] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [4] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [4] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [4] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [4] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [4] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [4] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [4] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [4] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [4] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [4] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [4] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [4] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [4] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [4] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [4] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [4] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [4] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [4] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [4] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [4] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [4] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [4] (data from MRSA252)
    SACOL1722(tig)trigger factor  [4] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [4] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [4] (data from MRSA252)
    SACOL0435GTP-dependent nucleic acid-binding protein EngD  [4] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [4] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [4] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [4] (data from MRSA252)
    SACOL1753universal stress protein  [4] (data from MRSA252)
    SACOL1759universal stress protein  [4] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [4] (data from MRSA252)
    SACOL2553pyruvate oxidase  [4] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [4] (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. ↑ 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)
  3. ↑ 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)
  4. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 4.46 4.47 4.48 4.49 4.50 4.51 4.52 4.53 4.54 4.55 4.56 4.57 4.58 4.59 4.60 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]

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