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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

General[edit source | edit]

  • 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 source | edit]

  • reaction:
  • TIGRFAM:
    Cellular processesCellular processesDetoxificationhydroxyacylglutathione hydrolase (TIGR03413; EC 3.1.2.6; HMM-score: 88.5)
    Unknown functionEnzymes of unknown specificityquinoprotein relay system zinc metallohydrolase 1 (TIGR04558; HMM-score: 29.1)
    Genetic information processingTranscriptionDegradation of RNAbeta-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 functionEnzymes of unknown specificityquinoprotein relay system zinc metallohydrolase 2 (TIGR04559; EC 3.-.-.-; HMM-score: 17.9)
    Genetic information processingTranscriptionRNA processingribonuclease Z (TIGR02651; EC 3.1.26.11; HMM-score: 16.4)
    Cellular processesCellular processesDNA transformationDNA internalization-related competence protein ComEC/Rec2 (TIGR00361; HMM-score: 12.9)
  • TheSEED:  
    Cobalt-zinc-cadmium resistance MBL-fold metallo-hydrolase superfamily 
    Glutathione: Non-redox reactions MBL-fold metallo-hydrolase superfamily 
    Glutathione-regulated potassium-efflux system and associated functions MBL-fold metallo-hydrolase superfamily 
    Methylglyoxal Metabolism MBL-fold metallo-hydrolase superfamily 
  • PFAM:
    Metallo-HOrase (CL0381) Lactamase_B; Metallo-beta-lactamase superfamily (PF00753; HMM-score: 118.1)
    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 definedDUF111; Protein of unknown function DUF111 (PF01969; HMM-score: 10.5)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL2657(arcA)arginine deiminase  [1] (data from MRSA252)
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [1] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [1] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [1] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [1] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.176
    • Ymax_pos: 24
    • Cmax: 0.211
    • Cmax_pos: 24
    • Smax: 0.235
    • Smax_pos: 17
    • Smean: 0.135
    • D: 0.16
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MRISSLTLGLVDTNTYFIENDKAVILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVKNGADKFKQYGLPIITSKVTPEKLNEGSTEIEGFKFNVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRTDLYKGDYETLVDSIQDKIFELEGDLPLFPGHGPYTTVDDEQLNPFLHG

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4]
    quantitative data / protein copy number per cell: 447 [5]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

Protein synthesis (provided by Aureolib)[edit source | edit]

Protein stability[edit source | edit]

  • half-life: 15.88 h [6]

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 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)
  2. 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)
  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. 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 source | edit]