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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
  • pan locus tag?: SAUPAN006297000
  • symbol: ldh2
  • pan gene symbol?: ldh2
  • synonym:
  • product: L-lactate dehydrogenase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
  • symbol: ldh2
  • product: L-lactate dehydrogenase
  • replicon: chromosome
  • strand: -
  • coordinates: 2674414..2675373
  • length: 960
  • 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
    ATGAAAACATTTGGTAAAAAGGTTGTATTAATCGGAGATGGATCTGTAGGATCAAGCTAT
    GCCTTTGCAATGGTTACGCAAGGTGTTGCTGATGAATTTGTAATTATTGACATTGCAAAA
    GACAAAGTAAAAGCAGATGTTCAAGATTTAAACCATGGTACAGTCCACAGTCCTTCACCA
    GTTGATGTGAAAGCAGGTGAATACGAAGACTGTAAAGATGCAGATTTAGTTGTTATTACA
    GCTGGCGCACCTCAAAAGCCAGGTGAAACACGTTTACAATTAGTTGAAAAAAATACTAAG
    ATTATGAAGAGCATCGTTAAGAGTGTTATGGATAGTGGCTTTGATGGATATTTCTTAATC
    GCGGCAAACCCTGTAGACATTTTAACAAGATTTGTAAAAGAATATACTGGATTACCAGCA
    GAGCGTGTTATCGGTTCAGGTACTGTATTGGACAGTGCACGTTTACAATATTTAATTAGC
    CAAGAACTTGGTGTTGCACCTTCAAGTGTTGACGCTAGTATTATTGGCGAGCATGGTGAT
    ACTGAACTTGCAGTTTGGTCACAAGCAAATGTAGCAGGTATTTCAGTATATGACACATTA
    AAAGAACAAACTGGTAGCGAAGCTAAAGCGGAAGAAATTTATGTGAATACACGTGACGCT
    GCTTATGAAATTATCCAAGCTAAAGGGTCAACATACTATGGTATTGCATTAGCATTGATG
    CGCATTTCAAAAGCCATTTTAAATAATGAAAATAATGTCTTAAATGTTTCTATACAATTA
    GATGGTCAATATGGTGGTCACAAAGGCGTTTACCTAGGTGTACCAACATTAGTTAACCAA
    CATGGCGCAGTTAAAATTTATGAAATGCCATTAAGTGCCGAAGAACAAGCGTTGTTCGAT
    AAATCTGTTAAAACATTAGAAGATACATTTGATTCAATTAAATATTTATTAGAAGACTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2618 [new locus tag: SACOL_RS13695 ]
  • symbol: Ldh2
  • description: L-lactate dehydrogenase
  • length: 319
  • theoretical pI: 4.53599
  • theoretical MW: 34419.8
  • GRAVY: -0.0498433

⊟Function[edit | edit source]

  • reaction:
    EC 1.1.1.27?  ExPASy
    L-lactate dehydrogenase (S)-lactate + NAD+ = pyruvate + NADH
  • TIGRFAM:
    Metabolism Energy metabolism Anaerobic L-lactate dehydrogenase (TIGR01771; EC 1.1.1.27; HMM-score: 420.6)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis L-lactate dehydrogenase (TIGR01771; EC 1.1.1.27; HMM-score: 420.6)
    and 9 more
    Metabolism Energy metabolism TCA cycle malate dehydrogenase, NAD-dependent (TIGR01763; EC 1.1.1.37; HMM-score: 209.2)
    Metabolism Energy metabolism TCA cycle malate dehydrogenase, NAD-dependent (TIGR01772; EC 1.1.1.37; HMM-score: 72.2)
    malate dehydrogenase (TIGR01759; EC 1.1.1.-; HMM-score: 68.5)
    lactate dehydrogenase (TIGR01756; EC 1.1.1.27; HMM-score: 51)
    malate dehydrogenase, NAD-dependent (TIGR01758; EC 1.1.1.37; HMM-score: 47.1)
    malate dehydrogenase, NADP-dependent (TIGR01757; EC 1.1.1.82; HMM-score: 17.8)
    Metabolism Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylD (TIGR03911; HMM-score: 15.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiazole biosynthesis adenylyltransferase ThiF (TIGR02356; EC 2.7.7.73; HMM-score: 12.4)
    nucleotide sugar dehydrogenase (TIGR03026; HMM-score: 12.2)
  • TheSEED  :
    • Malate dehydrogenase (EC 1.1.1.37)
    Carbohydrates Fermentation Fermentations: Lactate  L-lactate dehydrogenase (EC 1.1.1.27)
    and 1 more
    Carbohydrates Fermentation Fermentations: Mixed acid  L-lactate dehydrogenase (EC 1.1.1.27)
  • PFAM:
    NADP_Rossmann (CL0063) Ldh_1_N; lactate/malate dehydrogenase, NAD binding domain (PF00056; HMM-score: 153.1)
    and 5 more
    LDH_C (CL0341) Ldh_1_C; lactate/malate dehydrogenase, alpha/beta C-terminal domain (PF02866; HMM-score: 122.2)
    NADP_Rossmann (CL0063) Sacchrp_dh_NADP; Saccharopine dehydrogenase NADP binding domain (PF03435; HMM-score: 16.6)
    NAD_binding_7; Putative NAD(P)-binding (PF13241; HMM-score: 15.4)
    UDPG_MGDP_dh_N; UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain (PF03721; HMM-score: 15.2)
    F420_oxidored; NADP oxidoreductase coenzyme F420-dependent (PF03807; HMM-score: 14.9)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.108195
    • TAT(Tat/SPI): 0.002687
    • LIPO(Sec/SPII): 0.004804
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKTFGKKVVLIGDGSVGSSYAFAMVTQGVADEFVIIDIAKDKVKADVQDLNHGTVHSPSPVDVKAGEYEDCKDADLVVITAGAPQKPGETRLQLVEKNTKIMKSIVKSVMDSGFDGYFLIAANPVDILTRFVKEYTGLPAERVIGSGTVLDSARLQYLISQELGVAPSSVDASIIGEHGDTELAVWSQANVAGISVYDTLKEQTGSEAKAEEIYVNTRDAAYEIIQAKGSTYYGIALALMRISKAILNNENNVLNVSIQLDGQYGGHKGVYLGVPTLVNQHGAVKIYEMPLSAEEQALFDKSVKTLEDTFDSIKYLLED

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 812 [5]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [6] (data from MRSA252)
    SACOL0173(ipdC)indole-3-pyruvate decarboxylase  [6] (data from MRSA252)
    SACOL0033(mecA)penicillin-binding protein 2'  [6] (data from MRSA252)
    SACOL2272(modA)molybdenum ABC transporter molybdenum-binding protein ModA  [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)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL1277(pyrH)uridylate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL0439(rpsR)30S ribosomal protein S18  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [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)
    SACOL0599hypothetical protein  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [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: 38.03 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 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 6.46 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]

Anthony R Richardson, Stephen J Libby, Ferric C Fang
A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity.
Science: 2008, 319(5870);1672-6
[PubMed:18356528] [WorldCat.org] [DOI] (I p)

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