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NCBI: 03-AUG-2016

Summary[edit source | edit]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00538
  • pan locus tag?: SAUPAN002328000
  • symbol: SAOUHSC_00538
  • pan gene symbol?:
  • synonym:
  • product: haloacid dehalogenase-like hydrolase

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SAOUHSC_00538
  • symbol: SAOUHSC_00538
  • product: haloacid dehalogenase-like hydrolase
  • replicon: chromosome
  • strand: +
  • coordinates: 543109..543792
  • length: 684
  • essential: no DEG 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
    661
    ATGGAATGGATATTATTTGATAAAGATGGTACGTTAATTGAATTTGATAGAAGTTGGGAA
    AAAATAGGGGTACGATTTGTACAATCATTGCTTGAGACTTTCCCAGTACATAATAAAGAA
    GCTGCTTTAAGACAACTCGGTGTCATTAAAGAATCTATTGATCCAAAATCAGTGATGGGT
    TCAGGATCTTTACAACAAATTATCCAGGCATTTAATGATGTGACGGGACAAGATACAACC
    GACTGGTCCAAGTCAACAAGTCAAAAGCTGGTAGATGAACGTATTCCTGAAATTAATTGG
    GTAGAAGGTGTTAAAGAAGCACTTATCGATTTGAAAGCAAAAGGCTATCAACTTGGTATT
    GTTACGAGTGATACTAAAAAAGGTGTAGAACAATTTTTAGCACATACCAATGCTACCTCG
    TTGTTCGATTTGATCATTTCTACCGAAGCGGATGCCTATGAGAAGCCAAATCCTAAAGTA
    TTATCGCCTTTATTTGAGCAATATAATGTAGATCCTCAGAAAGTAGCTATAGTAGGAGAC
    ACTGCTAATGATATGAAGACAGCAAGTAATGCAAATTTAGGTATGGCAATAGGTGTATTA
    ACAGGTATTGCAACAAAAGAAGAATTACATGAAGCTGATATTATTTTAAATAGTGCGGCA
    GATATTTTAGAAGCTTTAAATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    684

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SAOUHSC_00538
  • symbol: SAOUHSC_00538
  • description: haloacid dehalogenase-like hydrolase
  • length: 227
  • theoretical pI: 4.35345
  • theoretical MW: 24992.1
  • GRAVY: -0.17489

Function[edit source | edit]

  • reaction:
  • TIGRFAM:
    HAD hydrolase, TIGR02253 family (TIGR02253; HMM-score: 70.8)
    MetabolismEnergy metabolismSugarsphosphoglycolate phosphatase, bacterial (TIGR01449; EC 3.1.3.18; HMM-score: 61.1)
    phosphonatase-like hydrolase (TIGR03351; HMM-score: 58.6)
    Unknown functionEnzymes of unknown specificityHAD hydrolase, family IIIA (TIGR01662; HMM-score: 54.9)
    Unknown functionEnzymes of unknown specificityHAD hydrolase, family IA, variant 1 (TIGR01549; HMM-score: 45.6)
    AHBA synthesis associated protein (TIGR01454; HMM-score: 42.9)
    HAD hydrolase, REG-2-like, family IA (TIGR02252; HMM-score: 41.7)
    histidinol-phosphate phosphatase domain (TIGR01656; HMM-score: 41.2)
    noncanonical pyrimidine nucleotidase, YjjG family (TIGR02254; EC 3.1.3.5; HMM-score: 38.5)
    haloacid dehalogenase, type II (TIGR01428; EC 3.8.1.2; HMM-score: 35.5)
    HAD hydrolase, TIGR01548 family (TIGR01548; HMM-score: 35.5)
    Cell structureCell envelopeBiosynthesis and degradation of surface polysaccharides and lipopolysaccharidesD,D-heptose 1,7-bisphosphate phosphatase (TIGR00213; HMM-score: 33.5)
    beta-phosphoglucomutase family hydrolase (TIGR02009; HMM-score: 31.2)
    MetabolismAmino acid biosynthesisSerine familyphosphoserine phosphatase SerB (TIGR00338; EC 3.1.3.3; HMM-score: 30.2)
    MetabolismEnergy metabolismBiosynthesis and degradation of polysaccharidesbeta-phosphoglucomutase (TIGR01990; EC 5.4.2.6; HMM-score: 29.2)
    MetabolismAmino acid biosynthesisHistidine familyhistidinol-phosphatase (TIGR01261; EC 3.1.3.15; HMM-score: 27.6)
    MetabolismCentral intermediary metabolismOtherphosphonoacetaldehyde hydrolase (TIGR01422; EC 3.11.1.1; HMM-score: 27.4)
    epoxide hydrolase N-terminal domain-like phosphatase (TIGR02247; HMM-score: 26.9)
    phosphoserine phosphatase-like hydrolase, archaeal (TIGR01491; HMM-score: 25.7)
    Unknown functionEnzymes of unknown specificityHAD phosphoserine phosphatase-like hydrolase, family IB (TIGR01488; HMM-score: 25.6)
    Unknown functionEnzymes of unknown specificityHAD hydrolase, family IA, variant 3 (TIGR01509; HMM-score: 24.8)
    HAD hydrolase, family IA, variant 2 (TIGR01493; HMM-score: 24)
    pyrimidine 5'-nucleotidase (TIGR01993; EC 3.1.3.5; HMM-score: 23)
    Cellular processesCellular processesDetoxificationcopper-translocating P-type ATPase (TIGR01511; EC 3.6.3.4; HMM-score: 21.9)
    MetabolismTransport and binding proteinsCations and iron carrying compoundscopper-translocating P-type ATPase (TIGR01511; EC 3.6.3.4; HMM-score: 21.9)
    heavy metal translocating P-type ATPase (TIGR01525; EC 3.6.3.-; HMM-score: 21)
    Unknown functionEnzymes of unknown specificityCof-like hydrolase (TIGR00099; HMM-score: 20.7)
    DNA 3'-phosphatase (TIGR01664; EC 3.1.3.32; HMM-score: 19.1)
    phosphoglycolate/pyridoxal phosphate phosphatase family (TIGR01452; EC 3.1.3.18; HMM-score: 17.4)
    phosphoglycolate phosphatase, TA0175-type (TIGR01487; EC 3.1.3.18; HMM-score: 15.9)
    Unknown functionEnzymes of unknown specificityHAD hydrolase, family IIB (TIGR01484; HMM-score: 14.6)
    HAD phosphatase, family IIIC (TIGR01681; HMM-score: 14.3)
    Cell structureCell envelopeBiosynthesis and degradation of surface polysaccharides and lipopolysaccharides3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family (TIGR01670; EC 3.1.3.45; HMM-score: 14.2)
    MetabolismTransport and binding proteinsCations and iron carrying compoundscadmium-translocating P-type ATPase (TIGR01512; EC 3.6.3.3; HMM-score: 13.1)
    HAD ATPase, P-type, family IC (TIGR01494; EC 3.6.3.-; HMM-score: 8.9)
  • TheSEED:  
    Hydrolase, haloacid dehalogenase-like family 
  • PFAM:
    HAD (CL0137) HAD_2; haloacid dehalogenase-like hydrolase (PF13419; HMM-score: 99.6)
    Hydrolase; haloacid dehalogenase-like hydrolase (PF00702; HMM-score: 65)
    Hydrolase_like; HAD-hyrolase-like (PF13242; HMM-score: 40)
    HAD; haloacid dehalogenase-like hydrolase (PF12710; HMM-score: 33)
    Hydrolase_3; haloacid dehalogenase-like hydrolase (PF08282; HMM-score: 23)
    Hydrolase_6; haloacid dehalogenase-like hydrolase (PF13344; HMM-score: 17.4)
    PNK3P; Polynucleotide kinase 3 phosphatase (PF08645; HMM-score: 16.7)
    Put_Phosphatase; Putative Phosphatase (PF06888; HMM-score: 13)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:

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: 0.128
    • Ymax_pos: 42
    • Cmax: 0.133
    • Cmax_pos: 42
    • Smax: 0.233
    • Smax_pos: 38
    • Smean: 0.072
    • D: 0.106
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MEWILFDKDGTLIEFDRSWEKIGVRFVQSLLETFPVHNKEAALRQLGVIKESIDPKSVMGSGSLQQIIQAFNDVTGQDTTDWSKSTSQKLVDERIPEINWVEGVKEALIDLKAKGYQLGIVTSDTKKGVEQFLAHTNATSLFDLIISTEADAYEKPNPKVLSPLFEQYNVDPQKVAIVGDTANDMKTASNANLGMAIGVLTGIATKEELHEADIILNSAADILEALN

Experimental data[edit source | edit]

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: no data available

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. Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  2. Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet.: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

Relevant publications[edit source | edit]