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NCBI: 02-MAR-2017

Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS05355 [old locus tag: SA0944 ]
  • pan locus tag?: SAUPAN003318000
  • symbol: SA_RS05355
  • pan gene symbol?: pdhB
  • synonym:
  • product: pyruvate dehydrogenase E1 component subunit beta

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SA_RS05355 [old locus tag: SA0944 ]
  • symbol: SA_RS05355
  • product: pyruvate dehydrogenase E1 component subunit beta
  • replicon: chromosome
  • strand: +
  • coordinates: 1071958..1072935
  • length: 978
  • essential: yes [1] DEG other strains

Accession numbers[edit | edit source]

  • Location: NC_002745 (1071958..1072935) NCBI
  • BioCyc: G1G21-1079 BioCyc
  • MicrobesOnline: see SA0944

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
    ATGGCACAAATGACAATGGTTCAAGCGATTAATGATGCGCTTAAAACTGAACTTAAAAAT
    GACCAAGATGTTTTAATTTTTGGTGAAGACGTTGGTGTTAACGGCGGTGTTTTCCGTGTT
    ACTGAAGGACTACAAAAAGAATTTGGTGAAGATAGAGTATTCGATACACCTTTAGCTGAA
    TCAGGTATTGGTGGTTTAGCGATGGGTCTTGCAGTTGAAGGATTCCGTCCGGTTATGGAA
    GTACAATTCTTAGGTTTCGTATTCGAAGTATTTGATGCGATTGCTGGACAAATTGCACGT
    ACTCGTTTCCGTTCAGGCGGTACTAAAACTGCACCTGTAACAATTCGTAGCCCATTTGGT
    GGTGGCGTACACACACCAGAATTACACGCAGATAACTTAGAAGGTATTTTAGCTCAATCT
    CCAGGTCTAAAGGTTGTTATTCCTTCAGGCCCATACGATGCGAAAGGTTTATTAATTTCT
    TCTATTAGAAGTAATGACCCAGTCGTATACTTAGAGCATATGAAATTGTATCGTTCATTC
    CGTGAAGAAGTACCTGAAGAAGAATATACAATTGACATTGGTAAGGCTAATGTGAAAAAA
    GAAGGTAATGACATTTCAATCATCACATACGGTGCAATGGTTCAAGAATCAATGAAAGCT
    GCAGAAGAACTTGAAAAAGATGGTTATTCTGTTGAAGTAATTGACTTACGTACTGTTCAA
    CCAATCGATGTTGACACAATTGTAGCTTCAGTTGAAAAAACTGGTCGTGCAGTTGTAGTT
    CAAGAAGCACAACGTCAAGCTGGTGTTGGTGCAGCAGTTGTAGCTGAATTAAGTGAACGT
    GCAATCCTTTCATTAGAAGCACCTATTGGAAGAGTTGCAGCAGCAGATACAATTTATCCA
    TTCACTCAAGCTGAAAATGTTTGGTTACCAAACAAAAATGACATCATCGAAAAAGCAAAA
    GAAACTTTAGAATTTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    978

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SA_RS05355 [old locus tag: SA0944 ]
  • symbol: SA_RS05355
  • description: pyruvate dehydrogenase E1 component subunit beta
  • length: 325
  • theoretical pI: 4.36436
  • theoretical MW: 35245.8
  • GRAVY: -0.0467692

Function[edit | edit source]

  • reaction:
    EC 1.2.4.1?  ExPASy
    Pyruvate dehydrogenase (acetyl-transferring) Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridoxine 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    and 2 more
    2-oxoacid:acceptor oxidoreductase, alpha subunit (TIGR03710; HMM-score: 25.6)
    pyruvate:ferredoxin (flavodoxin) oxidoreductase (TIGR02176; EC 1.2.7.1; HMM-score: 10.5)
  • TheSEED: see SA0944
  • PFAM:
    TKC_like (CL0591) Transketolase_C; Transketolase, C-terminal domain (PF02780; HMM-score: 135.3)
    THDP-binding (CL0254) Transket_pyr; Transketolase, pyrimidine binding domain (PF02779; HMM-score: 130.1)
    and 1 more
    TKC_like (CL0591) PFOR_II; Pyruvate:ferredoxin oxidoreductase core domain II (PF17147; HMM-score: 18.3)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors: thiamine diphosphate
  • effectors:

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • LocateP:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.004498
    • TAT(Tat/SPI): 0.000165
    • LIPO(Sec/SPII): 0.000333
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF

Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA_RS09855(gatA)glutamyl-tRNA(Gln) amidotransferase subunit A  [2] (data from MRSA252)
    SA_RS00310aminoglycoside O-nucleotidyltransferase ANT(4')-Ia  [2] (data from MRSA252)
    SA_RS01275formate acetyltransferase  [2] (data from MRSA252)
    SA_RS02005GTP-binding protein YchF  [2] (data from MRSA252)
    SA_RS0291050S ribosomal protein L1  [2] (data from MRSA252)
    SA_RS02955elongation factor G  [2] (data from MRSA252)
    SA_RS02960elongation factor Tu  [2] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [2] (data from MRSA252)
    SA_RS04710hypothetical protein  [2] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [2] (data from MRSA252)
    SA_RS05360dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  [2] (data from MRSA252)
    SA_RS05365dihydrolipoyl dehydrogenase  [2] (data from MRSA252)
    SA_RS05860cell division protein FtsZ  [2] (data from MRSA252)
    SA_RS0614050S ribosomal protein L19  [2] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [2] (data from MRSA252)
    SA_RS07060dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex  [2] (data from MRSA252)
    SA_RS070652-oxoglutarate dehydrogenase E1 component  [2] (data from MRSA252)
    SA_RS07205serine/threonine dehydratase  [2] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [2] (data from MRSA252)
    SA_RS07955molecular chaperone DnaK  [2] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [2] (data from MRSA252)
    SA_RS08430ATP-dependent Clp protease ATP-binding subunit ClpX  [2] (data from MRSA252)
    SA_RS0846050S ribosomal protein L20  [2] (data from MRSA252)
    SA_RS08505aldehyde dehydrogenase  [2] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [2] (data from MRSA252)
    SA_RS08560pyruvate kinase  [2] (data from MRSA252)
    SA_RS08625universal stress protein UspA  [2] (data from MRSA252)
    SA_RS0867530S ribosomal protein S4  [2] (data from MRSA252)
    SA_RS09850aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B  [2] (data from MRSA252)
    SA_RS10945UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [2] (data from MRSA252)
    SA_RS11060aldehyde dehydrogenase family protein  [2] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [2] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [2] (data from MRSA252)
    SA_RS1170550S ribosomal protein L5  [2] (data from MRSA252)
    SA_RS1172030S ribosomal protein S17  [2] (data from MRSA252)
    SA_RS1173530S ribosomal protein S3  [2] (data from MRSA252)
    SA_RS1174050S ribosomal protein L22  [2] (data from MRSA252)
    SA_RS1175050S ribosomal protein L2  [2] (data from MRSA252)
    SA_RS1175550S ribosomal protein L23  [2] (data from MRSA252)
    SA_RS1176050S ribosomal protein L4  [2] (data from MRSA252)
    SA_RS1176550S ribosomal protein L3  [2] (data from MRSA252)
    SA_RS13340pyruvate oxidase  [2] (data from MRSA252)
    SA_RS13420L-glutamate gamma-semialdehyde dehydrogenase  [2] (data from MRSA252)
    SA_RS13920arginine deiminase  [2] (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: 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. R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
    A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
    Mol Microbiol: 2002, 43(6);1387-400
    [PubMed:11952893] [WorldCat.org] [DOI] (P p)
  2. 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 2.29 2.30 2.31 2.32 2.33 2.34 2.35 2.36 2.37 2.38 2.39 2.40 2.41 2.42 2.43 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)

Relevant publications[edit | edit source]