From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2114 [new locus tag: SACOL_RS11060 ]
  • pan locus tag?: SAUPAN005414000
  • symbol: SACOL2114
  • pan gene symbol?: —
  • synonym:
  • product: aldehyde dehydrogenase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2114 [new locus tag: SACOL_RS11060 ]
  • symbol: SACOL2114
  • product: aldehyde dehydrogenase
  • replicon: chromosome
  • strand: -
  • coordinates: 2173813..2175240
  • length: 1428
  • 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
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    ATGAGAGACTACACAAAGCAATACATTAATGGCGAATGGGTAGAAAGTAATAGTAATGAA
    ACGATAGAAGTTATAAATCCAGCAACCGAAGAAGTAATCGGGAAAGTTGCTAAAGGTAAT
    AAAGCTGATGTTGATAAAGCCGTCGAGGCGGCAGACGATGTTTATTTAGAGTTCCGTCAT
    ACATCTGTGAAAGAAAGACAAGCGTTATTAGATAAAATTGTAAAAGAATATGAAAACAGA
    AAAGACGATATTGTACAAGCTATTACGGATGAATTAGGTGCTCCTTTATCATTATCTGAG
    CGTGTCCATTATCAAATGGGACTAAACCATTTTGTTGCAGCGAGAGACGCATTAGATAAC
    TACGAATTTGAAGAACGCCGCGGAGATGATTTAGTTGTTAAAGAAGCAATCGGTGTATCT
    GGATTAATTACACCGTGGAACTTCCCTACAAACCAAACATCATTAAAATTAGCAGCAGCA
    TTTGCGGCTGGTAGTCCAGTTGTACTTAAACCATCTGAAGAAACACCATTTGCAGCTGTT
    ATTTTAGCTGAGATTTTTGATAAAGTCGGTGTTCCTAAAGGTGTATTTAACCTTGTTAAT
    GGTGATGGTGCTGGTGTTGGGAATCCTTTATCTGAACATCCTAAAGTACGCATGATGTCA
    TTTACAGGATCAGGCCCTACTGGTTCTAAAATTATGGAAAAAGCCGCTAAAGATTTTAAA
    AAGGTATCATTAGAGCTTGGTGGCAAATCACCATATATCGTCCTAGATGACGTAGATATT
    AAAGAAGCGGCTAAAGCAACAACAGGCAAAGTTGTTAATAATACTGGTCAAGTATGTACA
    GCTGGTACACGTGTTTTAGTGCCTAACAAAATTAAAGATGCATTCTTAGCTGAATTAAAA
    GAACAATTTAGCCAAGTGCGTGTCGGTAATCCAAGAGAAGATGGTACACAAGTAGGCCCT
    ATCATTAGTAAAAAACAATTTGATCAAGTACAAAATTATATTAATAAAGGTATTGAAGAA
    GGTGCTGAATTATTTTATGGTGGTCCTGGTAAACCAGAAGGACTTGAAAAAGGATACTTT
    GCACGTCCGACAATTTTTATTAATGTAGATAATCAAATGACGATAGCACAAGAAGAAATT
    TTTGGGCCAGTAATGTCAGTTATCACTTATAACGATTTAGATGAAGCGATTCAAATTGCA
    AATGATACAAAATATGGTTTGGCAGGATATGTTATTGGTAAGGACAAAGAAACATTGCAT
    AAAGTAGCTCGTTCTATTGAAGCAGGTACAGTAGAAATAAACGAAGCAGGTAGAAAGCCA
    GATTTACCATTTGGTGGCTATAAACAATCTGGTTTAGGTCGTGAATGGGGCGATTATGGT
    ATTGAAGAGTTCTTAGAAGTGAAATCTATAGCTGGATATTTTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1428

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2114 [new locus tag: SACOL_RS11060 ]
  • symbol: SACOL2114
  • description: aldehyde dehydrogenase
  • length: 475
  • theoretical pI: 4.76962
  • theoretical MW: 51968.3
  • GRAVY: -0.350526

⊟Function[edit | edit source]

  • reaction:
    EC 1.2.1.3?  ExPASy
    Aldehyde dehydrogenase (NAD+) An aldehyde + NAD+ + H2O = a carboxylate + NADH
  • TIGRFAM:
    Cellular processes Cellular processes Adaptations to atypical conditions betaine-aldehyde dehydrogenase (TIGR01804; EC 1.2.1.8; HMM-score: 460)
    5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase (TIGR02299; EC 1.2.1.60; HMM-score: 449.2)
    Unknown function Enzymes of unknown specificity aldehyde dehydrogenase, Rv0768 family (TIGR04284; EC 1.2.1.-; HMM-score: 405)
    Metabolism Central intermediary metabolism Other succinate-semialdehyde dehydrogenase (TIGR01780; EC 1.2.1.-; HMM-score: 403.8)
    Metabolism Energy metabolism Other 2-hydroxymuconic semialdehyde dehydrogenase (TIGR03216; EC 1.2.1.-; HMM-score: 375.8)
    and 10 more
    Metabolism Energy metabolism Amino acids and amines putative delta-1-pyrroline-5-carboxylate dehydrogenase (TIGR01237; EC 1.2.1.88; HMM-score: 314.6)
    1-pyrroline dehydrogenase (TIGR03374; EC 1.2.1.19; HMM-score: 293.2)
    Metabolism Energy metabolism Amino acids and amines methylmalonate-semialdehyde dehydrogenase (acylating) (TIGR01722; EC 1.2.1.27; HMM-score: 274.6)
    putative phosphonoacetaldehyde dehydrogenase (TIGR03250; EC 1.2.1.-; HMM-score: 265.1)
    Metabolism Energy metabolism Amino acids and amines succinylglutamate-semialdehyde dehydrogenase (TIGR03240; EC 1.2.1.71; HMM-score: 223.8)
    Metabolism Energy metabolism Amino acids and amines delta-1-pyrroline-5-carboxylate dehydrogenase (TIGR01238; EC 1.2.1.88; HMM-score: 181.5)
    Metabolism Energy metabolism Amino acids and amines 1-pyrroline-5-carboxylate dehydrogenase (TIGR01236; EC 1.2.1.88; HMM-score: 169.2)
    phenylacetic acid degradation protein paaN (TIGR02278; HMM-score: 142.6)
    phenylacetic acid degradation protein paaN (TIGR02288; HMM-score: 48.8)
    acetaldehyde dehydrogenase (acetylating) (TIGR02518; EC 1.2.1.10; HMM-score: 23.1)
  • TheSEED  :
    • Aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3)
    Carbohydrates Central carbohydrate metabolism Methylglyoxal Metabolism  Aldehyde dehydrogenase (EC 1.2.1.3)
    and 2 more
    Carbohydrates Central carbohydrate metabolism Pyruvate metabolism II: acetyl-CoA, acetogenesis from pyruvate  Aldehyde dehydrogenase (EC 1.2.1.3)
    Fatty Acids, Lipids, and Isoprenoids Phospholipids Glycerolipid and Glycerophospholipid Metabolism in Bacteria  Aldehyde dehydrogenase (EC 1.2.1.3)
  • PFAM:
    ALDH-like (CL0099) Aldedh; Aldehyde dehydrogenase family (PF00171; HMM-score: 552.9)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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): 0.012993
    • TAT(Tat/SPI): 0.000365
    • LIPO(Sec/SPII): 0.000952
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MRDYTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIAGYFK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1853 [5]
  • interaction partners:
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: SigB* (activation) regulon
    SigB*(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation;  [7] [8]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟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. ↑ 6.0 6.1 6.2 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. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  8. ↑ Jan Pané-Farré, Beate Jonas, Konrad Förstner, Susanne Engelmann, Michael Hecker
    The sigmaB regulon in Staphylococcus aureus and its regulation.
    Int J Med Microbiol: 2006, 296(4-5);237-58
    [PubMed:16644280] [WorldCat.org] [DOI] (P p)

⊟Relevant publications[edit | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL2114&oldid=92083"