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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0584 [new locus tag: SACOL_RS03030 ]
  • pan locus tag?: SAUPAN002308000
  • symbol: rplA
  • pan gene symbol?: rplA
  • synonym:
  • product: 50S ribosomal protein L1

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0584 [new locus tag: SACOL_RS03030 ]
  • symbol: rplA
  • product: 50S ribosomal protein L1
  • replicon: chromosome
  • strand: +
  • coordinates: 604115..604807
  • length: 693
  • 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
    ATGGCTAAAAAAGGTAAAAAGTATCAAGAAGCAGCTAGTAAAGTTGACCGTACTCAGCAC
    TACAGTGTTGAAGAAGCAATTAAATTAGCTAAAGAAACAAGCATTGCTAACTTTGACGCT
    TCTGTTGAAGTTGCATTCCGTTTAGGAATTGATACACGTAAAAATGACCAACAAATCCGT
    GGTGCAGTTGTATTACCAAACGGAACTGGTAAATCACAAAGTGTATTAGTATTCGCTAAA
    GGTGACAAAATTGCTGAAGCTGAAGCAGCAGGTGCTGACTATGTAGGTGAAGCAGAATAC
    GTTCAAAAAATCCAACAAGGTTGGTTCGACTTCGATGTAGTAGTTGCTACACCAGACATG
    ATGGGTGAAGTTGGTAAATTAGGTCGTGTATTAGGACCAAAAGGTTTAATGCCAAACCCT
    AAAACTGGAACTGTAACAATGGATGTTAAAAAAGCTGTTGAAGAAATCAAAGCTGGTAAA
    GTAGAATATCGTGCTGAAAAAGCTGGTATCGTACATGCATCAATTGGTAAAGTTTCATTT
    ACTGATGAACAATTAATTGAAAACTTCAATACTTTACAAGATGTATTAGCTAAAGCTAAA
    CCATCATCTGCTAAAGGTACATACTTCAAATCTGTTGCTGTAACTACAACAATGGGTCCT
    GGAGTTAAAATTGATACTGCAAGTTTCAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    693

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0584 [new locus tag: SACOL_RS03030 ]
  • symbol: RplA
  • description: 50S ribosomal protein L1
  • length: 230
  • theoretical pI: 9.60658
  • theoretical MW: 24708.1
  • GRAVY: -0.29087

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL1 (TIGR01169; HMM-score: 352.6)
    and 1 more
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL1, mitochondrial (TIGR01170; HMM-score: 97.6)
  • TheSEED  :
    • LSU ribosomal protein L1p (L10Ae)
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L1p (L10Ae)
  • PFAM:
    no clan defined Ribosomal_L1; Ribosomal protein L1p/L10e family (PF00687; HMM-score: 185.5)
    and 2 more
    DUF3599; Domain of unknown function (DUF3599) (PF12206; HMM-score: 13)
    Patatin (CL0323) SAT; Starter unit:ACP transacylase in aflatoxin biosynthesis (PF16073; HMM-score: 11.6)

⊟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): 0.008938
    • TAT(Tat/SPI): 0.000654
    • LIPO(Sec/SPII): 0.000779
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKKGKKYQEAASKVDRTQHYSVEEAIKLAKETSIANFDASVEVAFRLGIDTRKNDQQIRGAVVLPNGTGKSQSVLVFAKGDKIAEAEAAGADYVGEAEYVQKIQQGWFDFDVVVATPDMMGEVGKLGRVLGPKGLMPNPKTGTVTMDVKKAVEEIKAGKVEYRAEKAGIVHASIGKVSFTDEQLIENFNTLQDVLAKAKPSSAKGTYFKSVAVTTTMGPGVKIDTASFK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 3831 [5]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [6] (data from MRSA252)
    SACOL1062(atl)bifunctional autolysin  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [6] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [6] (data from MRSA252)
    SACOL1317(glpP)glycerol uptake operon antiterminator regulatory protein  [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)
    SACOL1727(infC)translation initiation factor IF-3  [6] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL1837(metK)S-adenosylmethionine synthetase  [6] (data from MRSA252)
    SACOL2272(modA)molybdenum ABC transporter molybdenum-binding protein ModA  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL1390(parC)DNA topoisomerase IV subunit A  [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)
    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)
    SACOL2232(rplP)50S ribosomal protein L16  [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)
    SACOL2231(rpmC)50S ribosomal protein L29  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [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)
    SACOL0437(rpsF)30S ribosomal protein S6  [6] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [6] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [6] (data from MRSA252)
    SACOL0439(rpsR)30S ribosomal protein S18  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL1632(rpsU)30S ribosomal protein S21  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [6] (data from MRSA252)
    SACOL03035'-nucleotidase  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL1630hypothetical protein  [6] (data from MRSA252)
    SACOL1753universal stress protein  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL1788hypothetical protein  [6] (data from MRSA252)
    SACOL1789hypothetical protein  [6] (data from MRSA252)
    SACOL1897protein export protein PrsA  [6] (data from MRSA252)
    SACOL1994ABC transporter ATP-binding protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)
    SACOL2553pyruvate oxidase  [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: 13.04 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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 6.46 6.47 6.48 6.49 6.50 6.51 6.52 6.53 6.54 6.55 6.56 6.57 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]

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