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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2553 [new locus tag: SACOL_RS13365 ]
  • pan locus tag?: SAUPAN006196000
  • symbol: SACOL2553
  • pan gene symbol?: cidC
  • synonym:
  • product: pyruvate oxidase

⊟Additional information (user-provided)[edit | edit source]

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2553 [new locus tag: SACOL_RS13365 ]
  • symbol: SACOL2553
  • product: pyruvate oxidase
  • replicon: chromosome
  • strand: -
  • coordinates: 2611338..2613077
  • length: 1740
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟Additional information (user-provided)[edit | edit source]

⊟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
    1441
    1501
    1561
    1621
    1681
    ATGGCAAAAATAAAAGCAAATGAAGCATTAGTTAAAGCATTACAAGCATGGGATATAGAT
    CACTTGTATGGTATTCCAGGAGACTCAATCGACGCAGTAGTCGATAGTTTACGTACAGTG
    AGAGATCAATTTAAATTTTATCATGTACGTCATGAAGAAGTAGCAAGCTTAGCGGCTGCT
    GGTTACACAAAATTAACTGGTAAAATCGGTGTGGCATTAAGTATCGGTGGCCCTGGTTTA
    ATTCATTTATTAAATGGTATGTATGATGCCAAAATGGATAATGTACCGCAATTAATATTA
    TCTGGACAAACGAATAGTACAGCACTTGGAACGAAAGCATTCCAAGAAACAAATTTACAA
    AAATTATGTGAAGATGTAGCCGTTTATAATCACCAAATTGAAAAAGGTGACAATGTGTTT
    GAAATCGTTAACGAAGCAATTCGTACGGCATATGAACAAAAAGGTGTAGCTGTTGTTATT
    TGTCCTAACGACTTATTAACTGAAAAAATTAAAGATACAACGAATAAACCAGTAGATACA
    TCAAGACCAACAGTAGTATCACCAAAATATAAAGACATCAAAAAAGCGGTTAAACTAATT
    AATAAAAGTAAAAAGCCTGTCATGTTAATTGGTGTAGGTGCGAAACATGCGAAAGATGAG
    CTACGTGAATTTATTGAAATGGCTAAAATTCCTGTCATTCATTCATTACCAGCTAAAACA
    ATCTTGCCGGATGATCATCCATATAGTATCGGTAACTTAGGTAAAATCGGTACCAAAACA
    TCTTATCAAACAATGCAGGAAGCGGATTTATTAATTATGGTTGGTACAAACTATCCATAT
    GTGGATTACTTACCTAAGAAAAATATTAAAGCCATTCAAATTGACACAAATCCTAAAAAT
    ATCGGACATCGTTTCAATATTAATGTAGGAATTGTTGGAGATAGTAAAATTGCGTTGCAT
    CAGTTAACTGAAAATATTAAACATGTTGCTGAAAGACCATTCTTAAACAAAACGTTAGAA
    CGTAAAGCGGTTTGGGATAAATGGATGGAACAAGATAAAAATAATAATAGTAAACCATTA
    CGTCCAGAACGATTAATGGCATCAATCAATAAATTTATTAAAGATGATGCAGTGATTTCA
    GCAGATGTAGGTACAGCAACAGTTTGGTCAACTCGATACTTAAACCTTGGTGTAAATAAC
    AAGTTCATCATTTCAAGTTGGTTAGGTACAATGGGTTGCGGTCTTCCAGGTGCAATTGCA
    TCAAAAATTGCATATCCAAATAGACAAGCCATCGCAATTGCTGGTGACGGTGCATTCCAA
    ATGGTAATGCAAGACTTCGCTACAGCAGTACAATATGATTTACCTTTAACTGTATTTGTA
    CTTAATAACAAACAGTTAGCATTTATTAAATATGAACAACAAGCAGCTGGTGAATTAGAA
    TATGCAGTTGATTTTTCTGATATGGATCATGCAAAATTTGCTGAGGCAGCAGGTGGTAAA
    GGTTATACAATTAAGAGTGCTAGCGAAGTAGATGCTATAGTCGAAGAGGCATTAGCACAA
    GATGTACCAACGATTGTAGATGTATATGTTGATCCTAATGCTGCGCCATTACCAGGTAAA
    ATTGTAAATGAAGAAGCGCTTGGTTATGGTAAGTGGGCATTTAGATCAATTACTGAAGAT
    AAACATTTAGATTTAGATCAAATTCCACCAATTTCAGTGGCAGCAAAACGTTTCTTATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740


⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2553 [new locus tag: SACOL_RS13365 ]
  • symbol: SACOL2553
  • description: pyruvate oxidase
  • length: 579
  • theoretical pI: 7.43776
  • theoretical MW: 63756.9
  • GRAVY: -0.172193

⊟Function[edit | edit source]

  • reaction:
    EC 1.2.3.3?  ExPASy
    Pyruvate oxidase Pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
  • TIGRFAM:
    Metabolism Energy metabolism Aerobic pyruvate oxidase (TIGR02720; EC 1.2.3.3; HMM-score: 492.7)
    and 14 more
    Metabolism Amino acid biosynthesis Pyruvate family acetolactate synthase, large subunit, biosynthetic type (TIGR00118; EC 2.2.1.6; HMM-score: 367.2)
    Metabolism Energy metabolism Fermentation acetolactate synthase, catabolic (TIGR02418; EC 2.2.1.6; HMM-score: 270.3)
    Metabolism Central intermediary metabolism Other sulfoacetaldehyde acetyltransferase (TIGR03457; EC 2.3.3.15; HMM-score: 259)
    glyoxylate carboligase (TIGR01504; EC 4.1.1.47; HMM-score: 187.7)
    Cellular processes Cellular processes Detoxification oxalyl-CoA decarboxylase (TIGR03254; EC 4.1.1.8; HMM-score: 184.3)
    Metabolism Energy metabolism Sugars 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (TIGR04377; EC 3.7.1.-; HMM-score: 174.2)
    indolepyruvate/phenylpyruvate decarboxylase (TIGR03394; EC 4.1.1.43,4.1.1.74; HMM-score: 94.9)
    Metabolism Central intermediary metabolism Other indolepyruvate decarboxylase (TIGR03393; EC 4.1.1.74; HMM-score: 93.2)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase (TIGR00173; EC 2.2.1.9; HMM-score: 29)
    phosphonopyruvate decarboxylase (TIGR03297; EC 4.1.1.82; HMM-score: 27.5)
    sulfopyruvate decarboxylase, beta subunit (TIGR03846; EC 4.1.1.79; HMM-score: 20)
    Metabolism Energy metabolism Chemoautotrophy CO dehydrogenase/acetyl-CoA synthase complex, epsilon subunit (TIGR00315; EC 1.2.99.2; HMM-score: 15)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other sulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 14.6)
    Metabolism Energy metabolism Methanogenesis sulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 14.6)
  • TheSEED  :
    • Pyruvate oxidase [ubiquinone, cytochrome] (EC 1.2.2.2)
    • Pyruvate oxidase, CidC
    Carbohydrates Central carbohydrate metabolism Pyruvate metabolism II: acetyl-CoA, acetogenesis from pyruvate  Pyruvate oxidase [ubiquinone, cytochrome] (EC 1.2.2.2)
    and 1 more
    Regulation and Cell signaling Programmed Cell Death and Toxin-antitoxin Systems Murein hydrolase regulation and cell death  Pyruvate oxidase, CidC
  • PFAM:
    THDP-binding (CL0254) TPP_enzyme_C; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain (PF02775; HMM-score: 148.1)
    NADP_Rossmann (CL0063) TPP_enzyme_M; Thiamine pyrophosphate enzyme, central domain (PF00205; HMM-score: 128.7)
    and 4 more
    THDP-binding (CL0254) TPP_enzyme_N; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (PF02776; HMM-score: 99.8)
    POR_N; Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg (PF01855; HMM-score: 16)
    no clan defined PrpR_N; Propionate catabolism activator (PF06506; HMM-score: 13.5)
    NADP_Rossmann (CL0063) CO_dh; CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit (PF02552; HMM-score: 13.3)

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

  • domains:
  • modifications:
  • cofactors:
  • 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
  • DeepLocPro: Cytoplasmic Membrane
    • Cytoplasmic Score: 0.4823
    • Cytoplasmic Membrane Score: 0.4869
    • Cell wall & surface Score: 0.001
    • Extracellular Score: 0.0298
  • 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): 0.004655
    • TAT(Tat/SPI): 0.00018
    • LIPO(Sec/SPII): 0.000379
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Additional information (user-provided)[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQETNLQKLCEDVAVYNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLIGVGAKHAKDELREFIEMAKIPVIHSLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQEADLLIMVGTNYPYVDYLPKKNIKAIQIDTNPKNIGHRFNINVGIVGDSKIALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINKFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAIASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEALGYGKWAFRSITEDKHLDLDQIPPISVAAKRFL

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 650 [4]
  • interaction partners:
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [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)
    SACOL2239(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL1952ferritins family protein  [5] (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;  [6] [7]   other strains

⊟Additional information (user-provided)[edit | edit source]

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 24.74 h [8]

⊟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]

⊟Additional information (user-provided)[edit | edit source]

⊟Other information (user-provided)[edit | edit source]

You can add further information about the gene and protein here. [edit]

⊟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. ↑ 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 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. ↑ 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)
  7. ↑ 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)
  8. ↑ 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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