From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0922 [new locus tag: SACOL_RS04730 ]
  • pan locus tag?: SAUPAN003016000
  • symbol: SACOL0922
  • pan gene symbol?: —
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0922 [new locus tag: SACOL_RS04730 ]
  • symbol: SACOL0922
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 928830..929897
  • length: 1068
  • 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
    ATGTGGAATAAGAATCGACTTACTCAAATGTTAAGTATTGAATATCCAATTATACAAGCA
    GGTATGGCAGGAAGTACGACACCGAAATTAGTTGCATCAGTAAGTAACAGTGGTGGGTTA
    GGCACAATAGGCGCAGGTTACTTTAATACGCAGCAATTGGAAGATGAAATAGATTATGTA
    CGCCAATTAACGTCAAATTCTTTTGGCGTAAATGTCTTTGTACCAAGTCAACAATCATAT
    ACCAGTAGTCAAATTGAAAATATGAATGCATGGTTAAAACCTTATCGACGCGCATTACAT
    TTAGAAGAGCCGGTTGTAAAAATTACCGAAGAACAACAATTTAAGTGTCATATTGATACG
    ATAATTAAAAAGCAAGTGCCTGTATGTTGTTTTACTTTTGGAATTCCAAGCGAACAGATT
    ATAAGCAGGTTGAAAGCAGCGAATGTCAAACTTATAGGTACAGCAACAAGTGTTGATGAA
    GCTATTGCGAATGAAAAAGCGGGTATGGATGCTATCGTTGCTCAAGGTAGTGAAGCAGGT
    GGACATCGTGGTTCATTTTTAAAACCTAAAAATCAATTACCTATGGTTGGAACAATATCT
    TTAGTGCCACAAATTGTAGATGTCGTTTCAATTCCGGTCATTGCCGCTGGTGGAATTATG
    GATGGTAGAGGAGTTTTGGCAAGTATTGTCTTAGGTGCAGAAGGGGTACAAATGGGCACC
    GCATTTTTAACATCACAAGACAGTAATGCATCAGAACTACTGCGAGATGCAATTATAAAT
    AGTAAAGAAACAGATACAGTCATTACAAAAGCGTTTAGTGGAAAGCTTGCACGCGGTATC
    AACAATAGGTTTATCGAAGAAATGTCCCAATACGAAGGCGATATCCCAGATTATCCAATA
    CAAAATGAGCTAACAAGTAGCATAAGAAAAGCCGCAGCAAACATCGGCGACAAAGAGTTA
    ATACATATGTGGAGTGGACAAAGCCCGCGACTAGCAACAACGCATCCCGCCAACACCATC
    ATGTCCAATATAATCAATCAAATTAATCAAATCATGCAATATAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1068

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0922 [new locus tag: SACOL_RS04730 ]
  • symbol: SACOL0922
  • description: hypothetical protein
  • length: 355
  • theoretical pI: 6.36803
  • theoretical MW: 38547.8
  • GRAVY: -0.102535

⊟Function[edit | edit source]

  • reaction:
    EC 1.13.12.16?  ExPASy
    Nitronate monooxygenase Ethylnitronate + O2 = acetaldehyde + nitrite + other products
  • TIGRFAM:
    putative enoyl-[acyl-carrier-protein] reductase II (TIGR03151; EC 1.3.1.-; HMM-score: 233.2)
    and 8 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis inosine-5'-monophosphate dehydrogenase (TIGR01302; EC 1.1.1.205; HMM-score: 31.1)
    PfaD family protein (TIGR02814; HMM-score: 27.3)
    dihydroorotate dehydrogenase family protein (TIGR01037; EC 1.3.-.-; HMM-score: 24.6)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other isopentenyl-diphosphate delta-isomerase, type 2 (TIGR02151; EC 5.3.3.2; HMM-score: 18.8)
    Unknown function General IMP dehydrogenase family protein (TIGR01304; HMM-score: 17)
    heme/flavin dehydrogenase, mycofactocin system (TIGR03966; EC 1.-.-.-; HMM-score: 15.1)
    glycosyl amidation-associated protein WbuZ (TIGR03572; HMM-score: 12.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis dihydroorotate dehydrogenase (fumarate) (TIGR01036; EC 1.3.98.1; HMM-score: 11.8)
  • TheSEED  :
    • Enoyl-[acyl-carrier-protein] reductase [FMN] (EC 1.3.1.9)
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  Enoyl-[acyl-carrier-protein] reductase [FMN] (EC 1.3.1.9)
  • PFAM:
    TIM_barrel (CL0036) NMO; Nitronate monooxygenase (PF03060; HMM-score: 306.4)
    and 6 more
    IMPDH; IMP dehydrogenase / GMP reductase domain (PF00478; HMM-score: 33.5)
    FMN_dh; FMN-dependent dehydrogenase (PF01070; HMM-score: 29.6)
    Glu_synthase; Conserved region in glutamate synthase (PF01645; HMM-score: 22.6)
    DHO_dh; Dihydroorotate dehydrogenase (PF01180; HMM-score: 21.5)
    DUF561; Protein of unknown function (DUF561) (PF04481; HMM-score: 16.2)
    His_biosynth; Histidine biosynthesis protein (PF00977; HMM-score: 13.8)

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

  • domains:
  • modifications:
  • cofactors: FMN
  • 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: 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): 0.216307
    • TAT(Tat/SPI): 0.044046
    • LIPO(Sec/SPII): 0.078236
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MWNKNRLTQMLSIEYPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSQQSYTSSQIENMNAWLKPYRRALHLEEPVVKITEEQQFKCHIDTIIKKQVPVCCFTFGIPSEQIISRLKAANVKLIGTATSVDEAIANEKAGMDAIVAQGSEAGGHRGSFLKPKNQLPMVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNASELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEGDIPDYPIQNELTSSIRKAAANIGDKELIHMWSGQSPRLATTHPANTIMSNIINQINQIMQYK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SACOL1385(acnA)aconitate hydratase  [4] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [4] (data from MRSA252)
    SACOL2074(ddl)D-alanyl-alanine synthetase A  [4] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [4] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [4] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [4] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [4] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [4] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [4] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [4] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [4] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [4] (data from MRSA252)
    SACOL0544(prsA)ribose-phosphate pyrophosphokinase  [4] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [4] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [4] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [4] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [4] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [4] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [4] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [4] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [4] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [4] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [4] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [4] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [4] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [4] (data from MRSA252)
    SACOL0426acetyl-CoA acetyltransferase  [4] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [4] (data from MRSA252)
    SACOL0742hypothetical protein  [4] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [4] (data from MRSA252)
    SACOL1759universal stress protein  [4] (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 [5]   other strains

⊟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. ↑ 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, 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)
  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. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 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)
  5. ↑ 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)

⊟Relevant publications[edit | edit source]

Retrieved from "http://aureowiki.med.uni-greifswald.de/index.php?title=SACOL0922&oldid=74205"