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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 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
    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 source | edit]

General[edit source | edit]

  • 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 source | edit]

  • reaction:
    EC 1.2.3.3?  ExPASy
    Pyruvate oxidasePyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
  • TIGRFAM:
    MetabolismEnergy metabolismAerobicpyruvate oxidase (TIGR02720; EC 1.2.3.3; HMM-score: 492.7)
    MetabolismAmino acid biosynthesisPyruvate familyacetolactate synthase, large subunit, biosynthetic type (TIGR00118; EC 2.2.1.6; HMM-score: 367.2)
    MetabolismEnergy metabolismFermentationacetolactate synthase, catabolic (TIGR02418; EC 2.2.1.6; HMM-score: 270.3)
    MetabolismCentral intermediary metabolismOthersulfoacetaldehyde acetyltransferase (TIGR03457; EC 2.3.3.15; HMM-score: 259)
    glyoxylate carboligase (TIGR01504; EC 4.1.1.47; HMM-score: 187.7)
    Cellular processesCellular processesDetoxificationoxalyl-CoA decarboxylase (TIGR03254; EC 4.1.1.8; HMM-score: 184.3)
    MetabolismEnergy metabolismSugars3,5/4-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)
    MetabolismCentral intermediary metabolismOtherindolepyruvate decarboxylase (TIGR03393; EC 4.1.1.74; HMM-score: 93.2)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersMenaquinone and ubiquinone2-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)
    MetabolismEnergy metabolismChemoautotrophyCO dehydrogenase/acetyl-CoA synthase complex, epsilon subunit (TIGR00315; EC 1.2.99.2; HMM-score: 15)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersOthersulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 14.6)
    MetabolismEnergy metabolismMethanogenesissulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 14.6)
  • TheSEED:  
    CarbohydratesCentral carbohydrate metabolismPyruvate metabolism II: acetyl-CoA, acetogenesis from pyruvate Pyruvate oxidase [ubiquinone, cytochrome] (EC 1.2.2.2) 
    Regulation and Cell signalingProgrammed Cell Death and Toxin-antitoxin SystemsMurein 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: 138.5)
    TPP_enzyme_N; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (PF02776; HMM-score: 134.4)
    FAD_DHS (CL0085) TPP_enzyme_M; Thiamine pyrophosphate enzyme, central domain (PF00205; HMM-score: 117)
    THDP-binding (CL0254) POR_N; Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg (PF01855; HMM-score: 15.8)
    FAD_DHS (CL0085) CO_dh; CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit (PF02552; HMM-score: 13.7)
    no clan definedPrpR_N; Propionate catabolism activator (PF06506; HMM-score: 13.1)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL1513(hup)DNA-binding protein HU  [1] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [1] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [1] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [1] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [1] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [1] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [1] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [1] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [1] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [1] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [1] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [1] (data from MRSA252)
    SACOL1952ferritins family protein  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.107
    • Ymax_pos: 11
    • Cmax: 0.106
    • Cmax_pos: 25
    • Smax: 0.195
    • Smax_pos: 1
    • Smean: 0.094
    • D: 0.102
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQETNLQKLCEDVAVYNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLIGVGAKHAKDELREFIEMAKIPVIHSLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQEADLLIMVGTNYPYVDYLPKKNIKAIQIDTNPKNIGHRFNINVGIVGDSKIALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINKFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAIASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEALGYGKWAFRSITEDKHLDLDQIPPISVAAKRFL

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4]
    quantitative data / protein copy number per cell: 650 [5]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor: RpoF (SigB*) [6] [7] other strains
    RpoF  (SigB*) (sigma factor) controls a large regulon involved in stress/starvation response and adaptation
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 24.74 h [8]

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. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 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)
  2. 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)
  3. 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)
  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. 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)
  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. 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 source | edit]