From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1946 [new locus tag: SACOL_RS10175 ]
  • pan locus tag?: SAUPAN004903000
  • symbol: SACOL1946
  • pan gene symbol?: map
  • synonym:
  • product: methionine aminopeptidase

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1946 [new locus tag: SACOL_RS10175 ]
  • symbol: SACOL1946
  • product: methionine aminopeptidase
  • replicon: chromosome
  • strand: -
  • coordinates: 2007919..2008677
  • length: 759
  • 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
    ATGATTGTAAAAACAGAAGAAGAATTACAAGCGTTAAAAGAAATTGGATACATATGCGCT
    AAAGTGCGCAATACAATGCAAGCTGCAACCAAACCAGGTATCACTACGAAAGAGCTTGAT
    AATATTGCGAAAGAGTTATTTGAAGAATACGGTGCTATTTCTGCGCCAATTCATGATGAA
    AATTTTCCTGGTCAAACGTGTATTAGTGTCAATGAAGAGGTGGCACATGGGATTCCAAGT
    AAGCGTGTCATTCGTGAAGGAGATTTAGTAAATATTGATGTATCGGCTTTGAAGAATGGC
    TATTATGCAGATACAGGCATTTCATTTGTCGTTGGAGAATCAGATGATCCAATGAAACAA
    AAAGTATGTGACGTAGCAACGATGGCATTTGAGAATGCAATTGCAAAAGTAAAACCGGGT
    ACTAAGTTAAGTAACATTGGTAAAGCGGTGCATAATACAGCTAGACAAAATGATTTGAAA
    GTCATTAAAAACTTAACAGGTCATGGTGTTGGTTTATCATTACATGAAGCACCAGCACAT
    GTACTTAATTACTTTGATCCAAAAGACAAAACATTATTAACTGAAGGTATGGTATTAGCT
    ATTGAACCGTTTATCTCATCAAATGCATCATTTGTTACAGAAGGTAAAAATGAATGGGCT
    TTTGAAACGAGCGATAAAAGTTTTGTTGCTCAAATTGAGCATACGGTTATCGTGACTAAG
    GATGGTCCGATTTTAACGACAAAGATTGAAGAAGAATAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    759

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL1946 [new locus tag: SACOL_RS10175 ]
  • symbol: SACOL1946
  • description: methionine aminopeptidase
  • length: 252
  • theoretical pI: 4.93689
  • theoretical MW: 27502.1
  • GRAVY: -0.215476

Function[edit | edit source]

  • reaction:
    EC 3.4.11.18?  ExPASy
    Methionyl aminopeptidase Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
  • TIGRFAM:
    Genetic information processing Protein fate Protein modification and repair methionine aminopeptidase, type I (TIGR00500; EC 3.4.11.18; HMM-score: 282.6)
    and 3 more
    Genetic information processing Protein fate Protein modification and repair methionine aminopeptidase, type II (TIGR00501; EC 3.4.11.18; HMM-score: 110.5)
    Unknown function General DNA-binding protein, 42 kDa (TIGR00495; HMM-score: 53.2)
    ectoine utilization protein EutD (TIGR02993; EC 3.-.-.-; HMM-score: 11.5)
  • TheSEED  :
    • Methionine aminopeptidase (EC 3.4.11.18)
    Protein Metabolism Protein biosynthesis Translation termination factors bacterial  Methionine aminopeptidase (EC 3.4.11.18)
    and 1 more
    Protein Metabolism Protein degradation EC 3.4.11.- Aminopeptidases  Methionine aminopeptidase (EC 3.4.11.18)
  • PFAM:
    no clan defined Peptidase_M24; Metallopeptidase family M24 (PF00557; HMM-score: 168.1)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors: Co2+, Fe2+, Mn2+, Zn2+
  • 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): 0.011197
    • TAT(Tat/SPI): 0.001706
    • LIPO(Sec/SPII): 0.00293
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDENFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQKVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAHVLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTKDGPILTTKIEEE

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 381 [5]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL1759universal stress protein  [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: 45.17 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 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]