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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0461 [new locus tag: SACOL_RS02335 ]
  • pan locus tag?: SAUPAN001997000
  • symbol: guaA
  • pan gene symbol?: guaA
  • synonym:
  • product: GMP synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0461 [new locus tag: SACOL_RS02335 ]
  • symbol: guaA
  • product: GMP synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 463767..465308
  • length: 1542
  • 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
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    ATGGAAATGGCAAAAGAACAAGAGTTAATCCTTGTCTTAGACTTTGGTAGCCAATACAAC
    CAATTAATTACACGCCGAATTCGTGAAATGGGCGTTTATAGTGAATTACACGATCATGAA
    ATTTCAATTGAAGAAATTAAGAAAATGAATCCAAAAGGTATTATCTTATCAGGTGGTCCA
    AATTCAGTTTATGAAGAAGGTTCATTTACAATTGATCCGGAAATATATAATTTAGGAATT
    CCAGTACTTGGTATTTGTTACGGCATGCAATTAACTACTAAATTATTAGGTGGTAAAGTT
    GAACGTGCCAATGAACGTGAATACGGTAAAGCAATCATTAATGCGAAGTCAGATGAGTTA
    TTCGCTGGCTTACCAGCAGAACAAACTGTTTGGATGAGTCATTCTGATAAAGTTATTGAA
    ATTCCAGAAGGCTTTGAAGTTATCGCTGATAGCCCAAGCACAGACTATGCAGCAATCGAA
    GATAAGAAACGTCGCATTTATGGTGTTCAATTCCATCCAGAAGTACGTCATACAGAATAT
    GGTAATGATTTATTAAATAATTTTGTCCGTCGTGTTTGTGATTGTAGAGGTCAATGGACA
    ATGGAAAACTTTATCGAAATCGAAATTGAAAAGATTCGTCAACGCGTAGGAGACCGTCGT
    GTATTATGTGCGATGAGTGGCGGCGTAGATTCATCTGTTGTAGCTGTACTATTGCATAAA
    GCAATAGGTGATCAACTAACATGTATCTTTGTAGACCATGGCTTACTTCGTAAAGGTGAA
    GGCGACATGGTTATGGAGCAATTCGGTGAAGGTTTCAACATGAATATTATTCGTGTTAAT
    GCGAAAGATCGCTTTATGAATAAATTAAAAGGTGTTTCAGATCCTGAACAAAAACGTAAA
    ATCATTGGTAATGAATTTGTATACGTATTTGATGATGAAGCATCAAAACTGAAAGGTGTA
    GACTTCCTTGCGCAAGGAACACTATATACAGACGTCATCGAATCAGGTACTAAAACAGCA
    CAAACAATCAAATCACACCACAATGTTGGTGGATTACCAGAAGACATGGAATTCGAATTA
    ATCGAACCAATCAATACATTGTTTAAAGATGAAGTACGTAAATTAGGTATTGAGTTAGGT
    ATTCCAGAACATTTAGTATGGAGACAACCATTCCCAGGACCTGGTCTTGGTATTCGTGTA
    CTTGGAGAAATTACTGAAGATAAACTAGAAATCGTTAGAGAATCAGACGCGATTTTACGC
    CAAGTGATTAGAGAAGAAGGTCTTGAAAGAGAAATTTGGCAATACTTCACAGTGTTACCA
    AACATTCAATCAGTAGGTGTTATGGGAGACTACCGTACGTATGATCACACAGTAGGTATT
    CGTGCAGTAACATCTATCGACGGTATGACAAGTGACTTCGCACGCATCGATTGGGAAGTC
    TTACAAAAGATTTCTAGTCGTATCGTAAACGAAGTAGATCACGTCAACCGCGTAGTCTAT
    GACATTACATCAAAACCACCAAGCACAATTGAGTGGGAATAA
    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
    1542

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0461 [new locus tag: SACOL_RS02335 ]
  • symbol: GuaA
  • description: GMP synthase
  • length: 513
  • theoretical pI: 4.76247
  • theoretical MW: 58230
  • GRAVY: -0.289279

⊟Function[edit | edit source]

  • reaction:
    EC 6.3.5.2?  ExPASy
    GMP synthase (glutamine-hydrolyzing) ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis GMP synthase (glutamine-hydrolyzing), C-terminal domain (TIGR00884; EC 6.3.5.2; HMM-score: 508)
    and 13 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis GMP synthase (glutamine-hydrolyzing), N-terminal domain (TIGR00888; EC 6.3.5.2; HMM-score: 274.7)
    glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase (TIGR00566; HMM-score: 65.1)
    Metabolism Amino acid biosynthesis Aromatic amino acid family anthranilate synthase (TIGR01815; EC 4.1.3.27; HMM-score: 56.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, small subunit (TIGR01368; EC 6.3.5.5; HMM-score: 52.7)
    Metabolism Amino acid biosynthesis Histidine family imidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR01855; EC 2.4.2.-; HMM-score: 35.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides NAD+ synthetase (TIGR00552; EC 6.3.1.5; HMM-score: 35.6)
    aminodeoxychorismate synthase (TIGR01823; EC 2.6.1.85; HMM-score: 32)
    Hypothetical proteins Conserved TIGR00268 family protein (TIGR00268; HMM-score: 24.3)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (TIGR00420; EC 2.1.1.61; HMM-score: 20.4)
    Metabolism Amino acid biosynthesis Aspartate family asparagine synthase (glutamine-hydrolyzing) (TIGR01536; EC 6.3.5.4; HMM-score: 17.6)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA(Ile)-lysidine synthetase (TIGR02432; EC 6.3.4.-; HMM-score: 17.6)
    asparagine synthase family amidotransferase (TIGR03104; HMM-score: 14.6)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis CTP synthase (TIGR00337; EC 6.3.4.2; HMM-score: 12.2)
  • TheSEED  :
    • GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)
    Nucleosides and Nucleotides Purines Purine conversions  GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)
    and 1 more
    Phages, Prophages, Transposable elements, Plasmids Pathogenicity islands Staphylococcal pathogenicity islands SaPI  GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)
  • PFAM:
    Glutaminase_I (CL0014) GATase; Glutamine amidotransferase class-I (PF00117; HMM-score: 153.3)
    no clan defined GMP_synt_C; GMP synthase C terminal domain (PF00958; HMM-score: 144.7)
    and 8 more
    Glutaminase_I (CL0014) Peptidase_C26; Peptidase C26 (PF07722; HMM-score: 40.6)
    HUP (CL0039) NAD_synthase; NAD synthase (PF02540; HMM-score: 36.7)
    tRNA_Me_trans; tRNA methyl transferase (PF03054; HMM-score: 24.4)
    Asn_synthase; Asparagine synthase (PF00733; HMM-score: 21.4)
    ATP_bind_3; PP-loop family (PF01171; HMM-score: 19.3)
    QueC; Queuosine biosynthesis protein QueC (PF06508; HMM-score: 17.5)
    no clan defined LEA_6; Late embryogenesis abundant protein 18 (PF10714; HMM-score: 17)
    HUP (CL0039) PAPS_reduct; Phosphoadenosine phosphosulfate reductase family (PF01507; HMM-score: 12.8)

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

  • domains:
  • modifications:
  • cofactors:
  • 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): 0.00385
    • TAT(Tat/SPI): 0.00072
    • LIPO(Sec/SPII): 0.000338
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MEMAKEQELILVLDFGSQYNQLITRRIREMGVYSELHDHEISIEEIKKMNPKGIILSGGPNSVYEEGSFTIDPEIYNLGIPVLGICYGMQLTTKLLGGKVERANEREYGKAIINAKSDELFAGLPAEQTVWMSHSDKVIEIPEGFEVIADSPSTDYAAIEDKKRRIYGVQFHPEVRHTEYGNDLLNNFVRRVCDCRGQWTMENFIEIEIEKIRQRVGDRRVLCAMSGGVDSSVVAVLLHKAIGDQLTCIFVDHGLLRKGEGDMVMEQFGEGFNMNIIRVNAKDRFMNKLKGVSDPEQKRKIIGNEFVYVFDDEASKLKGVDFLAQGTLYTDVIESGTKTAQTIKSHHNVGGLPEDMEFELIEPINTLFKDEVRKLGIELGIPEHLVWRQPFPGPGLGIRVLGEITEDKLEIVRESDAILRQVIREEGLEREIWQYFTVLPNIQSVGVMGDYRTYDHTVGIRAVTSIDGMTSDFARIDWEVLQKISSRIVNEVDHVNRVVYDITSKPPSTIEWE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 3293 [5]
  • interaction partners:
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: G-box (transcription termination) regulon
    G-box(RNA)important in Purine metabolism; transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 78.87 h [7]

⊟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, 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. ↑ 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)
  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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 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)
  7. ↑ 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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