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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0846 [new locus tag: SACOL_RS04350 ]
  • pan locus tag?: SAUPAN002714000
  • symbol: SACOL0846
  • pan gene symbol?: rnr
  • synonym:
  • product: VacB/RNase II family exoribonuclease

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0846 [new locus tag: SACOL_RS04350 ]
  • symbol: SACOL0846
  • product: VacB/RNase II family exoribonuclease
  • replicon: chromosome
  • strand: +
  • coordinates: 873006..875378
  • length: 2373
  • 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
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    1681
    1741
    1801
    1861
    1921
    1981
    2041
    2101
    2161
    2221
    2281
    2341
    ATGAATTTAAAGCAATCTATAGAAGAGATTATTAATCAACCTGAATATGAACCTATGTCA
    GTGTCAGATTTTCAAGATGCATTAGGTTTAAGCAGTGCCGACTCGTTTAGAGATTTAATT
    AAGGTGCTTGTGGAGTTAGAACAATCAGGATTAATCGAACGTACAAAAACAGACAGATAC
    CAAAAAAAGCATAGTTATAGAGGTCAATCAAAATTGATAAAAGGAACGTTAAGTCAAAAT
    AAAAAAGGCTTTGCATTCTTAAGACCTGAAGATGAGGATATGGAAGATATATTTATTCCC
    CCGACGAAAATTAATCGTGCCTTGGATGGAGATACTGTTATTGTAGAAATCCATCAATCA
    AAAGGTGAACATAAAGGTAAAATCGAAGGGGAAGTTAAGTCGATTGAGAAGCATTCTGTA
    ACTCAAGTTGTTGGTACGTATAGTGAAGCTAGACATTTTGGCTTTGTTATTCCGGATGAT
    AAACGTATTATGCAAGATATTTTCATTCCTAAAGGTCAAAGTTTAGGCGCAGTCGATGGT
    CATAAGGTACTTGTACAAATTACTAAGTATGCTGATGGTTCAGATAATCCAGAAGGACAT
    ATTTCTGCTATTTTAGGACATAAAAATGATCCTGGCGTAGATATTTTATCTATTATCTAT
    CAACATGGCATAGAAATTGAATTTCCTGATGAAGTGTTACAAGAAGCTGAAGCAGTACCT
    GATCATATTGAAAATACTGAAATTAAAGGCCGTCATGATTTACGTGATGAATTGACAATC
    ACAATTGATGGTGCTGATGCTAAAGACTTAGATGACGCAATTAGTGTTAAAAAGTTAGCG
    AACGGTAATACGCAATTAACTGTAAGTATTGCTGATGTCAGCTATTATGTAACAGAAGGT
    TCTGCATTGGATAAAGAGGCATATGATAGAGCGACAAGTGTATATCTTGTTGACCGTGTA
    ATTCCAATGATTCCACATCGATTAAGTAATGGTATTTGTTCATTGAATCCTAATGTTGAT
    CGTTTAACTCTAAGCTGTCGCATGGAAATCGATGCTAGTGGTCGCGTTGTTAAACATGAA
    ATTTTTGATAGTGTTATACATTCTGATTATCGAATGACGTATGATGCGGTAAATCAGATT
    ATTACTGAAAAGGATCCTAACATTCGCGAACAATATAATGAAATTACGCCTATGCTAGAT
    TTAGCACAAGATTTATCTAATCGTTTGATTCAAATGAGAAAACGACGTGGTGAAATCGAT
    TTTGATATTAGTGAAGCAAAAGTATTAGTTAACGAAGACGGTATACCAACAGATGTTCAA
    TTAAGACAACGTGGCGAGGGTGAACGTCTAATTGAATCATTTATGTTAATTGCAAATGAA
    ACAGTTGCTGAACATTTTAGTAAGTTAGATGTACCTTTTATTTACCGAGTGCATGAGCAA
    CCTAAATCAGATCGCTTAAGACAATTCTTTGATTTTATTACAAACTTTGGCATCATGATT
    AAGGGTACTGGCGAAGATATTCATCCAACAACACTTCAAAAGGTTCAAGAAGAAGTAGAA
    GGTCGACCTGAACAAATGGTCATTTCAACAATGATGTTGCGTTCAATGCAACAAGCGCAT
    TATGATGATGTGAACTTGGGACATTTTGGCTTATCAGCTGAATATTATACGCATTTTACA
    TCACCAATTAGACGTTATCCTGATTTAACAGTTCATCGTTTAATCCGTAAGTATTTAATT
    GAGAAATCAATGGATAACAAAGAAGTGAAGCGTTGGGAAGACAAATTGCCTGAGTTAGCT
    GAACATACTTCTAAACGTGAACGTCGTGCTATTGAGGCAGAACGTGATACTGATGAATTG
    AAAAAAGCAGAATATATGATTCAACATATTGGTGATGAATTTGAAGGTATTGTCAGCTCA
    GTAGCTAACTTCGGTATGTTCATTGAATTGCCAAATACGATAGAAGGTATGGTTCATATT
    GCGAATATGACTGATGATTATTACCGTTTTGAAGAGCGTCAAATGGCATTAATTGGTGAG
    CGTCAAGCTAAAGTATTTAGAATTGGTGACACAGTTAAGGTTAAAGTGACGCATGTTGAT
    GTAGATGAACGATTAATTGATTTTCAAATTGTAGGTATGCCTTTACCGAAAAATGATCGA
    TCACAGCGCCCAGCGCGAGGTAAGACAATTCAAGCCAAAACGCGTGGTAAATCATTAGAT
    AAATCAAAATCTGATGATAAGGGTCGTAAGAAAAAAGGTAAGCAACGTAAAGGTAAAAAC
    CAACGTAATAATGATAAATCAGGTAATAGTAAGCATAAGCCATTTTATAAAGATAAAAGT
    GTGAAAAAGAAAGCACGTCGTAAGAAAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740
    1800
    1860
    1920
    1980
    2040
    2100
    2160
    2220
    2280
    2340
    2373

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL0846 [new locus tag: SACOL_RS04350 ]
  • symbol: SACOL0846
  • description: VacB/RNase II family exoribonuclease
  • length: 790
  • theoretical pI: 6.65179
  • theoretical MW: 90434.9
  • GRAVY: -0.672278

Function[edit | edit source]

  • reaction:
    EC 3.1.13.1?  ExPASy
    Exoribonuclease II Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
  • TIGRFAM:
    Genetic information processing Transcription Degradation of RNA ribonuclease R (TIGR02063; EC 3.1.-.-; HMM-score: 961.8)
    and 6 more
    Genetic information processing Transcription Degradation of RNA VacB and RNase II family 3'-5' exoribonucleases (TIGR00358; EC 3.1.13.1; HMM-score: 733.8)
    Genetic information processing Transcription Degradation of RNA exoribonuclease II (TIGR02062; EC 3.1.13.1; HMM-score: 206.2)
    Genetic information processing Transcription DNA-dependent RNA polymerase DNA-directed RNA polymerase (TIGR00448; EC 2.7.7.6; HMM-score: 40.7)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bS1 (TIGR00717; HMM-score: 30.4)
    Genetic information processing Transcription Degradation of RNA polyribonucleotide nucleotidyltransferase (TIGR03591; EC 2.7.7.8; HMM-score: 25.4)
    guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase (TIGR02696; EC 2.7.-.-,2.7.7.8; HMM-score: 14.7)
  • TheSEED  :
    • 3'-to-5' exoribonuclease RNase R
    RNA Metabolism RNA processing and modification RNA processing and degradation, bacterial  3'-to-5' exoribonuclease RNase R
  • PFAM:
    no clan defined RNB; RNB domain (PF00773; HMM-score: 372.5)
    and 6 more
    OB (CL0021) OB_RNB; Ribonuclease B OB domain (PF08206; HMM-score: 101)
    S1; S1 RNA binding domain (PF00575; HMM-score: 61.5)
    CSD; 'Cold-shock' DNA-binding domain (PF00313; HMM-score: 16.7)
    Rho_RNA_bind; Rho termination factor, RNA-binding domain (PF07497; HMM-score: 16)
    no clan defined MacB_PCD; MacB-like periplasmic core domain (PF12704; HMM-score: 13.5)
    HTH (CL0123) MarR; MarR family (PF01047; HMM-score: 12.4)

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): 0.003415
    • TAT(Tat/SPI): 0.001061
    • LIPO(Sec/SPII): 0.000359
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MNLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKHSYRGQSKLIKGTLSQNKKGFAFLRPEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGEHKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDDKRIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVPDHIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPNIREQYNEITPMLDLAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQFFDFITNFGIMIKGTGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIRKYLIEKSMDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIVGMPLPKNDRSQRPARGKTIQAKTRGKSLDKSKSDDKGRKKKGKQRKGKNQRNNDKSGNSKHKPFYKDKSVKKKARRKKK

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 154 [4]
  • interaction partners:
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [5] (data from MRSA252)
    SACOL0033(mecA)penicillin-binding protein 2'  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL03035'-nucleotidase  [5] (data from MRSA252)
    SACOL1098hypothetical protein  [5] (data from MRSA252)
    SACOL1426hypothetical protein  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL1975nicotinate phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL2072DEAD/DEAH box helicase  [5] (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: 50.3 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. 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 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)
  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]