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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0552 [new locus tag: SACOL_RS02825 ]
  • pan locus tag?: SAUPAN002249000
  • symbol: SACOL0552
  • pan gene symbol?:
  • synonym:
  • product: hypothetical protein

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0552 [new locus tag: SACOL_RS02825 ]
  • symbol: SACOL0552
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 561042..561443
  • length: 402
  • 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
    ATGTCAATCGAAGTTGGAAATAAGCTTAAAGGTAAAGTCACTGGTATTAAAAAGTTTGGT
    GCATTCGTAGAATTACCTGAAGGAAAAAGTGGTTTAGTTCACATTAGTGAAGTCGCAGAT
    AATTATGTTGAAAACGTAGAAGAGCACCTTTCTGTTGGTGATGAAGTAGACGTAAAAGTA
    TTATCTATTGCTGATGATGGAAAAATTAGTCTTTCAATTAAGAAAGCTAAAGACCGTCCA
    CGTAGACAACATACGAGTAAACCAAGTCATCAAAAACCAGTGCAAAAAGCCGAAGATTTT
    GAAAAGAAATTAAGCAATTTCTTAAAAGATAGTGAAGATAAATTAACTTCAATCAAACGT
    CAAACAGAATCTAGACGCGGTGGCAAAGGTTCAAGACGTTAA
    60
    120
    180
    240
    300
    360
    402

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL0552 [new locus tag: SACOL_RS02825 ]
  • symbol: SACOL0552
  • description: hypothetical protein
  • length: 133
  • theoretical pI: 10.3587
  • theoretical MW: 14811.7
  • GRAVY: -0.873684

Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Transcription Degradation of RNA polyribonucleotide nucleotidyltransferase (TIGR03591; EC 2.7.7.8; HMM-score: 75.4)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bS1 (TIGR00717; HMM-score: 69.5)
    and 7 more
    guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase (TIGR02696; EC 2.7.-.-,2.7.7.8; HMM-score: 47.4)
    Genetic information processing Transcription Degradation of RNA ribonuclease R (TIGR02063; EC 3.1.-.-; HMM-score: 36.6)
    Genetic information processing Transcription Degradation of RNA VacB and RNase II family 3'-5' exoribonucleases (TIGR00358; EC 3.1.13.1; HMM-score: 24.2)
    Genetic information processing Transcription Degradation of RNA ribonuclease, Rne/Rng family (TIGR00757; EC 3.1.4.-; HMM-score: 18.6)
    Genetic information processing Transcription DNA-dependent RNA polymerase DNA-directed RNA polymerase (TIGR00448; EC 2.7.7.6; HMM-score: 18.3)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis carbon storage regulator (TIGR00202; HMM-score: 14.2)
    Signal transduction Regulatory functions RNA interactions carbon storage regulator (TIGR00202; HMM-score: 14.2)
  • TheSEED:  
    Cell division-ribosomal stress proteins cluster  RNA binding protein, contains ribosomal protein S1 domain
  • PFAM:
    OB (CL0021) S1; S1 RNA binding domain (PF00575; HMM-score: 74.6)
    and 2 more
    S1_2; S1 domain (PF13509; HMM-score: 14.2)
    no clan defined CsrA; Global regulator protein family (PF02599; HMM-score: 12.7)

Structure, modifications & interactions[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL1513(hup)DNA-binding protein HU  [1] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [1] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [1] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [1] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [1] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [1] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [1] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [1] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [1] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [1] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [1] (data from MRSA252)
    SACOL1753universal stress protein  [1] (data from MRSA252)
    SACOL2325LysR family transcriptional regulator  [1] (data from MRSA252)

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.002975
    • TAT(Tat/SPI): 0.000161
    • LIPO(Sec/SPII): 0.000482
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MSIEVGNKLKGKVTGIKKFGAFVELPEGKSGLVHISEVADNYVENVEEHLSVGDEVDVKVLSIADDGKISLSIKKAKDRPRRQHTSKPSHQKPVQKAEDFEKKLSNFLKDSEDKLTSIKRQTESRRGGKGSRR

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4]
    quantitative data / protein copy number per cell: 569 [5]

Expression & Regulation[edit | edit source]

Operon[edit | edit source]

  • SACOL0552 no polycistronic organisation predicted

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: 11.33 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. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 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)
  2. 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)
  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. 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]