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NCBI: 26-AUG-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA2022 [new locus tag: SA_RS11630 ]
  • pan locus tag?: SAUPAN005675000
  • symbol: rplQ
  • pan gene symbol?: rplQ
  • synonym:
  • product: 50S ribosomal protein L17

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SA2022 [new locus tag: SA_RS11630 ]
  • symbol: rplQ
  • product: 50S ribosomal protein L17
  • replicon: chromosome
  • strand: -
  • coordinates: 2294726..2295094
  • length: 369
  • essential: yes [1] DEG 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
    ATGGGTTACAGAAAATTAGGTCGTACTTCTGATCAACGTAAAGCTATGTTACGTGACTTA
    GCTACATCACTTATTATTAGTGAACGTATTGAAACTACAGAAGCTCGTGCAAAAGAAGTT
    CGCAGTGTTGTTGAGAAATTAATCACTTTAGGTAAAAAAGGAGATTTAGCTTCTCGTCGT
    AATGCAGCTAAAACTTTACGTAATGTTGAAATCTTAAACGAAGATGAAACTACACAAACT
    GCACTTCAAAAATTATTTGGTGAAATCGCAGAGCGTTACACAGAACGTCAAGGTGGTTAC
    ACTCGTATCCTTAAACAAGGCCCTCGTCGCGGTGACGGTGCTGAATCAGTAATTATCGAA
    TTAGTATAA
    60
    120
    180
    240
    300
    360
    369

Protein[edit | edit source]

Protein Data Bank: 4WCE
Protein Data Bank: 4WF9
Protein Data Bank: 4WFA
Protein Data Bank: 4WFB
Protein Data Bank: 5HKV
Protein Data Bank: 5HL7
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5NRG
Protein Data Bank: 5TCU

General[edit | edit source]

  • locus tag: SA2022 [new locus tag: SA_RS11630 ]
  • symbol: RplQ
  • description: 50S ribosomal protein L17
  • length: 122
  • theoretical pI: 10.4546
  • theoretical MW: 13747.6
  • GRAVY: -0.622131

Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bL17 (TIGR00059; HMM-score: 146.1)
  • TheSEED  :
    • LSU ribosomal protein L17p
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L17p
  • PFAM:
    no clan defined Ribosomal_L17; Ribosomal protein L17 (PF01196; HMM-score: 126.3)
    and 1 more
    DUF4172; Domain of unknown function (DUF4172) (PF13776; HMM-score: 12.5)

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): 0.04315
    • TAT(Tat/SPI): 0.0108
    • LIPO(Sec/SPII): 0.002675
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MGYRKLGRTSDQRKAMLRDLATSLIISERIETTEARAKEVRSVVEKLITLGKKGDLASRRNAAKTLRNVEILNEDETTQTALQKLFGEIAERYTERQGGYTRILKQGPRRGDGAESVIIELV

Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA0366(ahpC)alkyl hydroperoxide reductase  [2] (data from MRSA252)
    SA1234(cspA)cold-shock protein CspA  [2] (data from MRSA252)
    SA1927(fbaA)fructose-bisphosphate aldolase  [2] (data from MRSA252)
    SA1112(infB)translation initiation factor IF-2  [2] (data from MRSA252)
    SA1244(odhB)dihydrolipoamide succinyltransferase  [2] (data from MRSA252)
    SA0934(ptsH)phosphocarrier protein HPr  [2] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [2] (data from MRSA252)
    SA2046(rplD)50S ribosomal protein L4  [2] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [2] (data from MRSA252)
    SA0497(rplJ)50S ribosomal protein L10  [2] (data from MRSA252)
    SA0495(rplK)50S ribosomal protein L11  [2] (data from MRSA252)
    SA2017(rplM)50S ribosomal protein L13  [2] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [2] (data from MRSA252)
    SA2040(rplP)50S ribosomal protein L16  [2] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [2] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [2] (data from MRSA252)
    SA2045(rplW)50S ribosomal protein L23  [2] (data from MRSA252)
    SA2023(rpoA)DNA-directed RNA polymerase subunit alpha  [2] (data from MRSA252)
    SA0500(rpoB)DNA-directed RNA polymerase subunit beta  [2] (data from MRSA252)
    SAS052(rpsD)30S ribosomal protein S4  [2] (data from MRSA252)
    SA0504(rpsG)30S ribosomal protein S7  [2] (data from MRSA252)
    SA2016(rpsI)30S ribosomal protein S9  [2] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [2] (data from MRSA252)
    SA0107(spa)immunoglobulin G binding protein A  [2] (data from MRSA252)
    SA0719(trxB)thioredoxine reductase  [2] (data from MRSA252)
    SA0477pyridoxal biosynthesis lyase PdxS  [2] (data from MRSA252)
    SA0627hypothetical protein  [2] (data from MRSA252)
    SA1272alanine dehydrogenase  [2] (data from MRSA252)
    SA1359elongation factor P  [2] (data from MRSA252)

Expression & Regulation[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. R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
    A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
    Mol Microbiol: 2002, 43(6);1387-400
    [PubMed:11952893] [WorldCat.org] [DOI] (P p)
  2. 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 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]