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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1655 [new locus tag: SACOL_RS08440 ]
  • pan locus tag?: SAUPAN004185000
  • symbol: mtn
  • pan gene symbol?: mtnN
  • synonym:
  • product: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1655 [new locus tag: SACOL_RS08440 ]
  • symbol: mtn
  • product: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
  • replicon: chromosome
  • strand: -
  • coordinates: 1683859..1684545
  • length: 687
  • 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
    ATGATTGGTATAATTGGTGCCATGGAAGAAGAAGTAACAATATTAAAAAATAAATTAACA
    CAATTAAGCGAAATTTCAGTTGCACATGTTAAATTTTATACTGGCATTTTAAAAGATAGA
    GAAGTAGTGATTACCCAAAGTGGCATTGGAAAAGTTAATGCTGCAATTTCTACGACATTA
    TTAATTAATAAGTTTAAACCGGACGTCATTATTAATACAGGTTCTGCTGGAGCTTTAGAT
    GAAAGTTTAAATGTAGGTGACGTTCTTATAAGTGATGATGTAAAATATCATGATGCAGAC
    GCAACAGCATTTGGTTATGAATATGGACAAATACCACAGATGCCGGTAGCATTTCAATCA
    AGTAAACCTTTAATAGAAAAAGTATCTCAAGTTGTACAACAACAACAATTAACAGCTAAA
    GTAGGCTTAATTGTAAGTGGTGATAGCTTTATCGGTAGTGTTGAACAACGCCAAAAAATT
    AAAAAAGCATTTCCAAATGCGATGGCGGTTGAAATGGAAGCAACTGCAATTGCACAAACA
    TGTTATCAATTTAATGTACCATTTGTTGTAGTTCGTGCAGTTTCAGACTTAGCAAATGGA
    GAAGCGGAAATGAGCTTCGAAGCATTTTTAGAAAAAGCAGCTGTATCATCAAGTCAAACT
    GTTGAAGCATTAGTGTCTCAATTATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    687

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1655 [new locus tag: SACOL_RS08440 ]
  • symbol: Mtn
  • description: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
  • length: 228
  • theoretical pI: 4.55905
  • theoretical MW: 24534
  • GRAVY: 0.183772

⊟Function[edit | edit source]

  • reaction:
    EC 3.2.2.9?  ExPASy
    Adenosylhomocysteine nucleosidase S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
    EC 3.2.2.16  ExPASy
    Methylthioadenosine nucleosidase S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine?
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides MTA/SAH nucleosidase (TIGR01704; EC 3.2.2.16,3.2.2.9; HMM-score: 297.3)
    Metabolism Central intermediary metabolism Other MTA/SAH nucleosidase (TIGR01704; EC 3.2.2.16,3.2.2.9; HMM-score: 297.3)
    and 10 more
    futalosine hydrolase (TIGR03664; EC 3.2.2.26; HMM-score: 90.6)
    hopanoid-associated phosphorylase (TIGR03468; HMM-score: 78.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides purine nucleoside phosphorylase (TIGR00107; EC 2.4.2.1; HMM-score: 61.6)
    putative 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (TIGR01705; HMM-score: 52.4)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides uridine phosphorylase (TIGR01718; EC 2.4.2.3; HMM-score: 33.8)
    AMP nucleosidase (TIGR01717; EC 3.2.2.4; HMM-score: 31.6)
    putative AMP nucleosidase (TIGR01721; HMM-score: 25.5)
    inosine/guanosine/xanthosine phosphorylase family (TIGR01697; EC 2.4.2.1; HMM-score: 18)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides methylthioadenosine phosphorylase (TIGR01694; EC 2.4.2.28; HMM-score: 15.1)
    Metabolism Central intermediary metabolism Other methylthioadenosine phosphorylase (TIGR01694; EC 2.4.2.28; HMM-score: 15.1)
  • TheSEED  :
    • 5'-methylthioadenosine nucleosidase (EC 3.2.2.16)
    • S-adenosylhomocysteine nucleosidase (EC 3.2.2.9)
    Amino Acids and Derivatives Arginine; urea cycle, polyamines Polyamine Metabolism  5'-methylthioadenosine nucleosidase (EC 3.2.2.16)
    and 2 more
    Amino Acids and Derivatives Lysine, threonine, methionine, and cysteine Methionine Biosynthesis  S-adenosylhomocysteine nucleosidase (EC 3.2.2.9)
    Amino Acids and Derivatives Lysine, threonine, methionine, and cysteine Methionine Degradation  S-adenosylhomocysteine nucleosidase (EC 3.2.2.9)
  • PFAM:
    PUP (CL0408) PNP_UDP_1; Phosphorylase superfamily (PF01048; HMM-score: 171.1)
    and 1 more
    no clan defined DNA_Packaging_2; DNA packaging protein (PF11123; HMM-score: 14.5)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • 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): 0.002526
    • TAT(Tat/SPI): 0.000256
    • LIPO(Sec/SPII): 0.000288
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MIGIIGAMEEEVTILKNKLTQLSEISVAHVKFYTGILKDREVVITQSGIGKVNAAISTTLLINKFKPDVIINTGSAGALDESLNVGDVLISDDVKYHDADATAFGYEYGQIPQMPVAFQSSKPLIEKVSQVVQQQQLTAKVGLIVSGDSFIGSVEQRQKIKKAFPNAMAVEMEATAIAQTCYQFNVPFVVVRAVSDLANGEAEMSFEAFLEKAAVSSSQTVEALVSQL

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 539 [4]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL0660(adhP)alcohol dehydrogenase  [5] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [5] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL2654(arcC2)carbamate kinase  [5] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [5] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0988(fabF)3-oxoacyl-ACP synthase  [5] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [5] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [5] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [5] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [5] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL2092(murAA)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [5] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [5] (data from MRSA252)
    SACOL1011(ppnK)inorganic polyphosphate/ATP-NAD kinase  [5] (data from MRSA252)
    SACOL0539(purR)pur operon repressor  [5] (data from MRSA252)
    SACOL1816(putA)proline dehydrogenase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [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)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2229(rplN)50S ribosomal protein L14  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [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)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [5] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [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)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [5] (data from MRSA252)
    SACOL1377(tkt)transketolase  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL03035'-nucleotidase  [5] (data from MRSA252)
    SACOL0727hypothetical protein  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [5] (data from MRSA252)
    SACOL1670hypothetical protein  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL1801dipeptidase PepV  [5] (data from MRSA252)
    SACOL1952ferritins family protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)
    SACOL2367alcohol dehydrogenase, zinc-containing  [5] (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: 40.56 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 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 5.51 5.52 5.53 5.54 5.55 5.56 5.57 5.58 5.59 5.60 5.61 5.62 5.63 5.64 5.65 5.66 5.67 5.68 5.69 5.70 5.71 5.72 5.73 5.74 5.75 5.76 5.77 5.78 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]

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