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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2313 [new locus tag: SACOL_RS12165 ]
  • pan locus tag?: SAUPAN005800000
  • symbol: SACOL2313
  • pan gene symbol?: —
  • synonym:
  • product: HAD superfamily hydrolase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2313 [new locus tag: SACOL_RS12165 ]
  • symbol: SACOL2313
  • product: HAD superfamily hydrolase
  • replicon: chromosome
  • strand: -
  • coordinates: 2373597..2374232
  • length: 636
  • 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
    ATGTATAGAGCAGTTATATTTGATTTCGATGGAACAATAATAGATACGGAACAACATTTA
    TTTAATGTTATTAATAAACATTTAGAGATGCATAATGCCGATCCTATAAGCATTGATTTT
    TATCGTTCTTCTATTGGAGGAGCAGCTACAGATTTGCATGACCATTTAATTAAAGCGATT
    GGTTCGGAAAATAAAGATAAACTTTATGAAGAACATCATCTTACTAGTACAACATTACCG
    ATGATTGATACGATTAAATCATTGATGGCATTTTTAAAGCAACGTCACATTCCTATGGCA
    ATTGCCACAAGTAGTGTGAAAGCGGAAATAATGCCCACCTTTAAAGCATTAGGTCTAGAC
    GATTATATAGAGGTAGTTGTTGGTAGAGAAGATGTTGAACAAGTTAAACCTGACCCTGAA
    TTATATTTATCTGCAGTACAACAATTAAATTATATGCCGACACAATGTTTGGCTATTGAA
    GATTCTGTAAATGGTGCAACAGCCGCGATTGCAGCTGGATTAGATGTTATTGTTAATACG
    AATAAAATGACAAGCGCACAGGACTTTTCTAATGTAGATTATGTAGCAAAAGATATTGAT
    TACGATCAAATTGTAGCGCGTTTCTTTACGAAATAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    636

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2313 [new locus tag: SACOL_RS12165 ]
  • symbol: SACOL2313
  • description: HAD superfamily hydrolase
  • length: 211
  • theoretical pI: 4.59654
  • theoretical MW: 23569.7
  • GRAVY: -0.0682464

⊟Function[edit | edit source]

  • TIGRFAM:
    beta-phosphoglucomutase family hydrolase (TIGR02009; HMM-score: 97.7)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides beta-phosphoglucomutase (TIGR01990; EC 5.4.2.6; HMM-score: 83.5)
    and 21 more
    Metabolism Energy metabolism Sugars phosphoglycolate phosphatase, bacterial (TIGR01449; EC 3.1.3.18; HMM-score: 75.6)
    Unknown function Enzymes of unknown specificity HAD hydrolase, family IA, variant 3 (TIGR01509; HMM-score: 64.3)
    HAD hydrolase, TIGR02253 family (TIGR02253; HMM-score: 57.4)
    AHBA synthesis associated protein (TIGR01454; HMM-score: 49.3)
    noncanonical pyrimidine nucleotidase, YjjG family (TIGR02254; EC 3.1.3.5; HMM-score: 40.5)
    pyrimidine 5'-nucleotidase (TIGR01993; EC 3.1.3.5; HMM-score: 37.9)
    haloacid dehalogenase, type II (TIGR01428; EC 3.8.1.2; HMM-score: 35.7)
    HAD hydrolase, REG-2-like, family IA (TIGR02252; HMM-score: 33.2)
    Unknown function Enzymes of unknown specificity HAD hydrolase, family IA, variant 1 (TIGR01549; HMM-score: 32)
    Metabolism Central intermediary metabolism Other 2,3-diketo-5-methylthio-1-phosphopentane phosphatase (TIGR01489; HMM-score: 29.6)
    Metabolism Central intermediary metabolism Other phosphonoacetaldehyde hydrolase (TIGR01422; EC 3.11.1.1; HMM-score: 28.1)
    phosphonatase-like hydrolase (TIGR03351; HMM-score: 26.9)
    Unknown function Enzymes of unknown specificity HAD phosphoserine phosphatase-like hydrolase, family IB (TIGR01488; HMM-score: 25.2)
    epoxide hydrolase N-terminal domain-like phosphatase (TIGR02247; HMM-score: 24.5)
    Unknown function Enzymes of unknown specificity HAD hydrolase, family IIIA (TIGR01662; HMM-score: 24.3)
    HAD hydrolase, TIGR01548 family (TIGR01548; HMM-score: 22.7)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides D,D-heptose 1,7-bisphosphate phosphatase (TIGR00213; HMM-score: 19.5)
    histidinol-phosphate phosphatase domain (TIGR01656; HMM-score: 17.3)
    HAD phosphatase, family IIIC (TIGR01681; HMM-score: 15.2)
    Unknown function Enzymes of unknown specificity HAD hydrolase, family IB (TIGR01490; HMM-score: 13.5)
    phosphoserine phosphatase-like hydrolase, archaeal (TIGR01491; HMM-score: 12.4)
  • TheSEED  :
    • Phosphoglycolate phosphatase
  • PFAM:
    HAD (CL0137) HAD_2; haloacid dehalogenase-like hydrolase (PF13419; HMM-score: 124.3)
    Hydrolase; haloacid dehalogenase-like hydrolase (PF00702; HMM-score: 100.6)
    and 3 more
    HAD; haloacid dehalogenase-like hydrolase (PF12710; HMM-score: 22.7)
    Hydrolase_like; HAD-hyrolase-like (PF13242; HMM-score: 18.8)
    Put_Phosphatase; Putative Phosphatase (PF06888; HMM-score: 14.8)

⊟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
  • DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9972
    • Cytoplasmic Membrane Score: 0.0008
    • Cell wall & surface Score: 0.0001
    • Extracellular Score: 0.0019
  • 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): 0.002671
    • TAT(Tat/SPI): 0.000207
    • LIPO(Sec/SPII): 0.000164
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MYRAVIFDFDGTIIDTEQHLFNVINKHLEMHNADPISIDFYRSSIGGAATDLHDHLIKAIGSENKDKLYEEHHLTSTTLPMIDTIKSLMAFLKQRHIPMAIATSSVKAEIMPTFKALGLDDYIEVVVGREDVEQVKPDPELYLSAVQQLNYMPTQCLAIEDSVNGATAAIAAGLDVIVNTNKMTSAQDFSNVDYVAKDIDYDQIVARFFTK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 328 [4]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [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)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [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)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [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: 39.27 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 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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