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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0944 [new locus tag: SACOL_RS04840 ]
  • pan locus tag?: SAUPAN003040000
  • symbol: SACOL0944
  • pan gene symbol?: ndh2a
  • synonym:
  • product: NADH dehydrogenase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0944 [new locus tag: SACOL_RS04840 ]
  • symbol: SACOL0944
  • product: NADH dehydrogenase
  • replicon: chromosome
  • strand: +
  • coordinates: 945411..946619
  • length: 1209
  • 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
    ATGGCTCAAGATCGTAAAAAAGTACTTGTACTTGGTGCTGGTTATGCAGGTTTACAAACT
    GTAACTAAATTGCAAAAAGCGATATCAACAGAAGAAGCAGAAATTACGCTTATTAATAAA
    AATGAATATCACTATGAAGCAACATGGTTACATGAAGCATCAGCAGGTACACTAAACTAT
    GAAGATGTATTATATCCTGTGGAAAGTGTCTTGAAGAAAGACAAAGTGAACTTTGTTCAA
    GCAGAAGTAACAAAAATTGACCGTGATGCTAAAAAGGTAGAAACAAATCAAGGTATTTAT
    GACTTTGATATTTTAGTAGTAGCATTAGGTTTCGTTAGTGAAACATTCGGCATCGAAGGT
    ATGAAAGATCATGCTTTCCAAATTGAAAATGTTATCACAGCACGTGAATTATCACGTCAT
    ATCGAAGACAAATTTGCTAACTATGCAGCATCAAAAGAAAAAGATGATAACGATTTATCT
    ATCTTAGTTGGTGGTGCTGGATTCACTGGTGTTGAATTCTTAGGTGAATTAACAGACAGA
    ATTCCTGAATTATGTAGCAAATATGGTGTGGATCAAAATAAAGTTAAAATCACTTGTGTT
    GAAGCAGCACCTAAAATGTTACCAATGTTCTCAGAAGAATTAGTTAACCACGCAGTTAGC
    TACTTAGAAGACCGCGGTGTTGAATTTAAAATTGCTACACCAATCGTTGCTTGTAACGAA
    AAAGGTTTTGTAGTTGAAGTAGATGGTGAAAAACAACAATTAAATGCAGGTACTTCAGTA
    TGGGCAGCTGGTGTACGTGGTAGTAAATTAATGGAAGAATCATTTGAAGGCGTTAAACGT
    GGACGTATCGTTACAAAGCAAGATTTAACAATCAATGGTTACGACAACATTTTTGTTATT
    GGTGACTGTTCAGCGTTTATCCCAGCTGGAGAAGAACGTCCATTACCAACTACAGCACAA
    ATTGCAATGCAACAAGGTGAAAGTGTTGCTAAAAACATTAAACGCATCTTAAACGGTGAA
    TCAACTGAAGAATTCGAATACGTTGATCGTGGAACTGTTTGTTCTTTAGGTTCACATGAC
    GGTGTAGGTATGGTATTTGGTAAACCTATCGCTGGTAAAAAAGCAGCATTCATGAAAAAA
    GTGATTGATACACGTGCGGTATTCAAAATCGGTGGTATCGGTTTAGCATTCAAAAAAGGT
    AAATTCTAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1209

⊟Protein[edit | edit source]

Protein Data Bank: 5NA1
Protein Data Bank: 5NA4

⊟General[edit | edit source]

  • locus tag: SACOL0944 [new locus tag: SACOL_RS04840 ]
  • symbol: SACOL0944
  • description: NADH dehydrogenase
  • length: 402
  • theoretical pI: 5.14656
  • theoretical MW: 44104.1
  • GRAVY: -0.176119

⊟Function[edit | edit source]

  • reaction:
    EC 1.6.99.-?  ExPASy
  • TIGRFAM:
    pyridine nucleotide-disulfide oxidoreductase family protein (TIGR03169; HMM-score: 96.8)
    and 7 more
    oxidoreductase/SelD-related fusion protein (TIGR04369; HMM-score: 61.7)
    Cellular processes Cellular processes Detoxification CoA-disulfide reductase (TIGR03385; EC 1.8.1.14; HMM-score: 53)
    dihydrolipoyl dehydrogenase (TIGR01350; EC 1.8.1.4; HMM-score: 33.4)
    Metabolism Central intermediary metabolism Nitrogen metabolism nitrite reductase [NAD(P)H], large subunit (TIGR02374; EC 1.7.1.4; HMM-score: 33.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine glycine oxidase ThiO (TIGR02352; EC 1.4.3.19; HMM-score: 17.4)
    putative alkyl hydroperoxide reductase F subunit (TIGR03143; EC 1.6.4.-; HMM-score: 16.6)
    glutamate synthase, NADH/NADPH, small subunit (TIGR01317; EC 1.4.1.-; HMM-score: 9.6)
  • TheSEED  :
    • NADH dehydrogenase (EC 1.6.99.3)
    Respiration Electron donating reactions Respiratory dehydrogenases 1  NADH dehydrogenase (EC 1.6.99.3)
  • PFAM:
    NADP_Rossmann (CL0063) Pyr_redox_2; Pyridine nucleotide-disulphide oxidoreductase (PF07992; HMM-score: 145.9)
    and 9 more
    Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase (PF00070; HMM-score: 37.5)
    DAO; FAD dependent oxidoreductase (PF01266; HMM-score: 29.6)
    NAD_binding_9; FAD-NAD(P)-binding (PF13454; HMM-score: 24.4)
    Sacchrp_dh_NADP; Saccharopine dehydrogenase NADP binding domain (PF03435; HMM-score: 15.7)
    NAD_binding_7; Putative NAD(P)-binding (PF13241; HMM-score: 13.5)
    AlaDh_PNT_C; Alanine dehydrogenase/PNT, C-terminal domain (PF01262; HMM-score: 12.7)
    Maf (CL0269) Ham1p_like; Ham1 family (PF01725; HMM-score: 12.7)
    NADP_Rossmann (CL0063) K_oxygenase; L-lysine 6-monooxygenase (NADPH-requiring) (PF13434; HMM-score: 12.6)
    no clan defined Tau95; RNA polymerase III transcription factor (TF)IIIC subunit (PF09734; HMM-score: 11.3)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 1.05
    • Cytoplasmic Membrane Score: 8.78
    • Cellwall Score: 0.08
    • Extracellular Score: 0.09
    • 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): 0.159156
    • TAT(Tat/SPI): 0.029488
    • LIPO(Sec/SPII): 0.008793
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAQDRKKVLVLGAGYAGLQTVTKLQKAISTEEAEITLINKNEYHYEATWLHEASAGTLNYEDVLYPVESVLKKDKVNFVQAEVTKIDRDAKKVETNQGIYDFDILVVALGFVSETFGIEGMKDHAFQIENVITARELSRHIEDKFANYAASKEKDDNDLSILVGGAGFTGVEFLGELTDRIPELCSKYGVDQNKVKITCVEAAPKMLPMFSEELVNHAVSYLEDRGVEFKIATPIVACNEKGFVVEVDGEKQQLNAGTSVWAAGVRGSKLMEESFEGVKRGRIVTKQDLTINGYDNIFVIGDCSAFIPAGEERPLPTTAQIAMQQGESVAKNIKRILNGESTEEFEYVDRGTVCSLGSHDGVGMVFGKPIAGKKAAFMKKVIDTRAVFKIGGIGLAFKKGKF

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 2324 [5]
  • interaction partners:
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (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: 32.37 h [7]

⊟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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 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. ↑ 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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