From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1602 [new locus tag: SACOL_RS08170 ]
  • pan locus tag?: SAUPAN004124000
  • symbol: SACOL1602
  • pan gene symbol?: —
  • synonym:
  • product: metallo-beta-lactamase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1602 [new locus tag: SACOL_RS08170 ]
  • symbol: SACOL1602
  • product: metallo-beta-lactamase
  • replicon: chromosome
  • strand: -
  • coordinates: 1634303..1634926
  • length: 624
  • 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
    ATGAGGATTTCAAGCTTAACTTTAGGCTTAGTTGATACTAATACGTATTTCATCGAAAAT
    GACAAAGCTGTTATTCTGATTGACCCTTCAGGTGAAAGTGAAAAAATTATTAAAAAATTA
    AACCAAATAAATAAACCGTTAAAAGCTATTTTATTAACACATGCACACTTTGATCATATC
    GGAGCAGTCGATGATATAGTTGATCGATTCGATGTCCCGGTTTATATGCATGAAGCAGAG
    TTTGATTTTCTAAAAGATCCCGTTAAAAATGGGGCAGATAAATTTAAGCAATATGGATTA
    CCAATTATTACAAGTAAGGTAACTCCTGAAAAGTTAAACGAAGGTAGCACAGAAATAGAA
    GGATTTAAGTTTAATGTGTTACACACACCTGGACATTCACCAGGAAGTTTAACATATGTG
    TTCGATGAATTCGCAGTTGTTGGAGATACATTATTTAATAATGGAATCGGACGTACAGAT
    TTATATAAAGGTGATTATGAAACGCTAGTTGATTCTATTCAAGATAAAATATTTGAATTA
    GAAGGCGATTTACCTTTATTCCCTGGACATGGTCCATATACGACGGTTGATGATGAACAA
    TTAAATCCATTTTTACACGGTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    624

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1602 [new locus tag: SACOL_RS08170 ]
  • symbol: SACOL1602
  • description: metallo-beta-lactamase
  • length: 207
  • theoretical pI: 4.50237
  • theoretical MW: 23140.9
  • GRAVY: -0.248792

⊟Function[edit | edit source]

  • TIGRFAM:
    Cellular processes Cellular processes Detoxification hydroxyacylglutathione hydrolase (TIGR03413; EC 3.1.2.6; HMM-score: 88.5)
    and 6 more
    Unknown function Enzymes of unknown specificity quinoprotein relay system zinc metallohydrolase 1 (TIGR04558; HMM-score: 29.1)
    Genetic information processing Transcription Degradation of RNA beta-CASP ribonuclease, RNase J family (TIGR00649; EC 3.1.-.-; HMM-score: 26.8)
    arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein (TIGR03675; HMM-score: 19.3)
    Unknown function Enzymes of unknown specificity quinoprotein relay system zinc metallohydrolase 2 (TIGR04559; EC 3.-.-.-; HMM-score: 17.9)
    Genetic information processing Transcription RNA processing ribonuclease Z (TIGR02651; EC 3.1.26.11; HMM-score: 16.4)
    Cellular processes Cellular processes DNA transformation DNA internalization-related competence protein ComEC/Rec2 (TIGR00361; HMM-score: 12.9)
  • TheSEED  :
    • MBL-fold metallo-hydrolase superfamily
    Carbohydrates Central carbohydrate metabolism Methylglyoxal Metabolism  Hydroxyacylglutathione hydrolase (EC 3.1.2.6)
    and 3 more
    Potassium metabolism Potassium metabolism - no subcategory Glutathione-regulated potassium-efflux system and associated functions  Hydroxyacylglutathione hydrolase (EC 3.1.2.6)
    Stress Response Oxidative stress Glutathione: Non-redox reactions  Hydroxyacylglutathione hydrolase (EC 3.1.2.6)
    Virulence, Disease and Defense Resistance to antibiotics and toxic compounds Cobalt-zinc-cadmium resistance  Hydroxyacylglutathione hydrolase (EC 3.1.2.6)
  • PFAM:
    Metallo-HOrase (CL0381) Lactamase_B; Metallo-beta-lactamase superfamily (PF00753; HMM-score: 118.1)
    and 6 more
    Lactamase_B_2; Beta-lactamase superfamily domain (PF12706; HMM-score: 30.9)
    Lactamase_B_3; Beta-lactamase superfamily domain (PF13483; HMM-score: 23.5)
    Lactamase_B_6; Metallo-beta-lactamase superfamily domain (PF16661; HMM-score: 23.3)
    PDEase_II; cAMP phosphodiesterases class-II (PF02112; HMM-score: 13.6)
    HEXAPEP (CL0536) Fucokinase; L-fucokinase (PF07959; HMM-score: 13.5)
    no clan defined DUF111; Protein of unknown function DUF111 (PF01969; HMM-score: 10.5)

⊟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): 0.00551
    • TAT(Tat/SPI): 0.000077
    • LIPO(Sec/SPII): 0.000417
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MRISSLTLGLVDTNTYFIENDKAVILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVKNGADKFKQYGLPIITSKVTPEKLNEGSTEIEGFKFNVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRTDLYKGDYETLVDSIQDKIFELEGDLPLFPGHGPYTTVDDEQLNPFLHG

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 447 [4]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [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: 15.88 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. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 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]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1602&oldid=83895"