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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0877 [new locus tag: SACOL_RS04500 ]
  • pan locus tag?: SAUPAN002821000
  • symbol: gcvH
  • pan gene symbol?: gcvH
  • synonym:
  • product: glycine cleavage system protein H

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0877 [new locus tag: SACOL_RS04500 ]
  • symbol: gcvH
  • product: glycine cleavage system protein H
  • replicon: chromosome
  • strand: +
  • coordinates: 897692..898072
  • length: 381
  • 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
    TTGGCAGTACCAAATGAATTGAAATATTCAAAAGAGCATGAATGGGTTAAAGTTGAAGGT
    AATGTAGCAATAATTGGAATCACAGAATACGCACAAAGCGAGTTAGGTGATATTGTTTTC
    GTTGAATTACCAGAAACAGATGATGAAATTAATGAAGGGGATACGTTTGGTAGCGTAGAA
    TCAGTTAAAACTGTATCAGAATTATATGCACCAATCTCTGGTAAAGTAGTTGAAGTCAAC
    GAAGAACTAGAAGATAGTCCCGAATTTGTAAATGAATCTCCATACGAAAAAGCATGGATG
    GTAAAAGTAGAAATTAGTGATGAAAGTCAGATTGAAGCTTTATTAACAGCTGAAAAATAT
    TCAGAAATGATTGGTGAATAA
    60
    120
    180
    240
    300
    360
    381

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0877 [new locus tag: SACOL_RS04500 ]
  • symbol: GcvH
  • description: glycine cleavage system protein H
  • length: 126
  • theoretical pI: 3.70004
  • theoretical MW: 14092.5
  • GRAVY: -0.333333

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Amino acids and amines glycine cleavage system H protein (TIGR00527; HMM-score: 184.5)
    and 3 more
    glycine cleavage protein H-like protein (TIGR03077; HMM-score: 69.5)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 15.2)
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 11.1)
  • TheSEED  :
    • Glycine cleavage system H protein
    Amino Acids and Derivatives Alanine, serine, and glycine Glycine and Serine Utilization  Glycine cleavage system H protein
    and 1 more
    Amino Acids and Derivatives Alanine, serine, and glycine Glycine cleavage system  Glycine cleavage system H protein
  • PFAM:
    Hybrid (CL0105) GCV_H; Glycine cleavage H-protein (PF01597; HMM-score: 164.8)
    and 2 more
    Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 16.5)
    RnfC_N; RnfC Barrel sandwich hybrid domain (PF13375; HMM-score: 16.4)

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

  • domains:
  • modifications:
  • cofactors: (R)-lipoate
  • 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): 0.003128
    • TAT(Tat/SPI): 0.000167
    • LIPO(Sec/SPII): 0.000284
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAVPNELKYSKEHEWVKVEGNVAIIGITEYAQSELGDIVFVELPETDDEINEGDTFGSVESVKTVSELYAPISGKVVEVNEELEDSPEFVNESPYEKAWMVKVEISDESQIEALLTAEKYSEMIGE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 2826 [4]
  • interaction partners:
    SACOL2656(arcB2)ornithine carbamoyltransferase  [5] (data from MRSA252)
    SACOL1595(gcvT)glycine cleavage system aminomethyltransferase T  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [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)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [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)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL1726(rpmI)50S ribosomal protein L35  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL1020hypothetical protein  [5] (data from MRSA252)
    SACOL1593glycine dehydrogenase subunit 2  [5] (data from MRSA252)
    SACOL1594glycine dehydrogenase subunit 1  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CcpA regulon
    CcpA(TF)important in Carbon catabolism; RegPrecise 

⊟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. ↑ 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 5.26 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]

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