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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • pan locus tag?: SAUPAN003287000
  • symbol: purD
  • pan gene symbol?: purD
  • synonym:
  • product: phosphoribosylamine--glycine ligase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • symbol: purD
  • product: phosphoribosylamine--glycine ligase
  • replicon: chromosome
  • strand: +
  • coordinates: 1092909..1094156
  • length: 1248
  • 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
    ATGAATGTATTAGTAATTGGTGCTGGTGGACGAGAACATGCACTTGCATATAAACTTAAT
    CAATCGAATCTAGTTAAACAAGTGTTTGTCATTCCAGGTAATGAGGCAATGACACCTATA
    GCTGAAGTACACACTGAAATTTCAGAACCTGATCATCAAGCGATACTAGATTTTGCTAAA
    CGGCAAAATGTTGATTGGGTAGTTATAGGTCCAGAACAGCCGCTAATTGATGGATTAGCA
    GACATTTTACGAGCGAATGGTTTCAAAGTGTTTGGTCCAAATAAGCAAGCAGCTCAAATC
    GAAGGCTCAAAATTATTTGCTAAAAAGATAATGGAAAAATATAATATTCCAACTGCTGAT
    TATAAAGAAGTTGAGCGAAAAAAGGATGCTTTAACATATATTGAAAACTGTGAATTGCCC
    GTTGTTGTCAAGAAAGATGGGTTAGCTGCTGGGAAAGGCGTTATTATTGCAGATACTATT
    GAAGCAGCCAGAAGTGCTATTGAGATTATGTATGGTGATGAAGAAGAAGGTACTGTTGTA
    TTTGAAACGTTTTTAGAAGGTGAAGAGTTCTCGCTAATGACATTTGTTAATGGTGATTTA
    GCAGTACCTTTCGACTGTATTGCACAAGATCATAAACGCGCATTTGATCATGATGAAGGA
    CCAAATACTGGTGGTATGGGGGCTTATTGTCCAGTACCACATATTAGTGACGATGTTTTA
    AAACTTACAAATGAAACAATTGCACAACCCATTGCAAAGGCAATGCTTAATGAAGGTTAT
    CAATTCTTCGGTGTATTATACATTGGTGCTATTTTAACTAAAGATGGTCCAAAAGTAATA
    GAATTTAATGCCCGTTTTGGTGATCCTGAAGCTCAAGTATTATTAAGTCGCATGGAAAGT
    GATTTAATGCAGCATATTATTGATTTAGATGAAGGAAAACGTACTGAATTCAAATGGAAA
    AATGAATCTATTGTAGGGGTCATGTTGGCATCAAAAGGATATCCTGATGCATATGAAAAA
    GGGCATAAAGTAAGTGGCTTTGATTTAAATGAAAACTATTTTGTTAGTGGATTAAAGAAG
    CAAGGTGATACCTTTGTTACTTCAGGTGGTAGAGTTATACTTGCCATCGGAAAAGGTGAC
    AATGTACAAGATGCACAGCGAGACGCATACAAAAAAGTATCACAAATACAAAGTGACCAT
    TTATTCTATCGTCATGACATTGCGAATAAAGCACTACAACTTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1248

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • symbol: PurD
  • description: phosphoribosylamine--glycine ligase
  • length: 415
  • theoretical pI: 4.89379
  • theoretical MW: 45858.9
  • GRAVY: -0.244819

⊟Function[edit | edit source]

  • ⊞⊞reaction:
    EC 6.3.4.13?  ExPASy
    Phosphoribosylamine--glycine ligase ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
  • ⊞⊞TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylamine--glycine ligase (TIGR00877; EC 6.3.4.13; HMM-score: 466)
    and 11 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, large subunit (TIGR01369; EC 6.3.5.5; HMM-score: 36.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazole carboxylase, ATPase subunit (TIGR01161; EC 4.1.1.21; HMM-score: 29.2)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan D-alanine--D-alanine ligase (TIGR01205; EC 6.3.2.4; HMM-score: 28.3)
    Cellular processes Cellular processes Biosynthesis of natural products cyanophycin synthetase (TIGR02068; EC 6.3.2.29,6.3.2.30; HMM-score: 24.7)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 22.4)
    alpha-L-glutamate ligase, RimK family (TIGR00768; EC 6.3.2.-; HMM-score: 22.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylglycinamide formyltransferase 2 (TIGR01142; EC 2.1.2.-; HMM-score: 19.4)
    Metabolism Energy metabolism TCA cycle succinate-CoA ligase, beta subunit (TIGR01016; EC 6.2.1.-; HMM-score: 14.6)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 14.2)
    Metabolism Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylC (TIGR03909; HMM-score: 13.7)
    lysine biosynthesis enzyme LysX (TIGR02144; HMM-score: 13.1)
  • ⊞⊞TheSEED  :
    • Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
    Miscellaneous Miscellaneous - no subcategory EC 6.3.4.- Ligases that form carbon-nitrogen bonds  Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
    and 1 more
    Nucleosides and Nucleotides Purines De Novo Purine Biosynthesis  Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
  • ⊞⊞PFAM:
    ATP-grasp (CL0179) GARS_A; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain (PF01071; HMM-score: 228.6)
    and 10 more
    NADP_Rossmann (CL0063) GARS_N; Phosphoribosylglycinamide synthetase, N domain (PF02844; HMM-score: 125.6)
    Hybrid (CL0105) GARS_C; Phosphoribosylglycinamide synthetase, C domain (PF02843; HMM-score: 86.6)
    ATP-grasp (CL0179) ATP-grasp_3; ATP-grasp domain (PF02655; HMM-score: 29.8)
    ATP-grasp; ATP-grasp domain (PF02222; HMM-score: 24.6)
    RimK; RimK-like ATP-grasp domain (PF08443; HMM-score: 17.5)
    ATP-grasp_5; ATP-grasp domain (PF13549; HMM-score: 16.7)
    Dala_Dala_lig_C; D-ala D-ala ligase C-terminus (PF07478; HMM-score: 16.6)
    CPSase_L_D2; Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786; HMM-score: 15.9)
    MurF-HprK_N (CL0365) Mur_ligase; Mur ligase family, catalytic domain (PF01225; HMM-score: 15.8)
    ATP-grasp (CL0179) ATP-grasp_2; ATP-grasp domain (PF08442; HMM-score: 13.6)

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

  • domains:
  • modifications:
  • cofactors: Mg2+, Mn2+
  • 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
  • ⊞⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9929
    • Cytoplasmic Membrane Score: 0.0005
    • Cell wall & surface Score: 0.0003
    • Extracellular Score: 0.0063
  • ⊞⊞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): 0.008564
    • TAT(Tat/SPI): 0.000596
    • LIPO(Sec/SPII): 0.001631
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNVLVIGAGGREHALAYKLNQSNLVKQVFVIPGNEAMTPIAEVHTEISEPDHQAILDFAKRQNVDWVVIGPEQPLIDGLADILRANGFKVFGPNKQAAQIEGSKLFAKKIMEKYNIPTADYKEVERKKDALTYIENCELPVVVKKDGLAAGKGVIIADTIEAARSAIEIMYGDEEEGTVVFETFLEGEEFSLMTFVNGDLAVPFDCIAQDHKRAFDHDEGPNTGGMGAYCPVPHISDDVLKLTNETIAQPIAKAMLNEGYQFFGVLYIGAILTKDGPKVIEFNARFGDPEAQVLLSRMESDLMQHIIDLDEGKRTEFKWKNESIVGVMLASKGYPDAYEKGHKVSGFDLNENYFVSGLKKQGDTFVTSGGRVILAIGKGDNVQDAQRDAYKKVSQIQSDHLFYRHDIANKALQLK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1731 [5]
  • ⊟⊟interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [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)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL1753universal stress protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • data available for N315

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 25.44 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. ↑ Jump up to: 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 6.17 6.18 6.19 6.20 6.21 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]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1083&oldid=91126"
Insert paragraph

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • pan locus tag?: SAUPAN003287000
  • symbol: purD
  • pan gene symbol?: purD
  • synonym:
  • product: phosphoribosylamine--glycine ligase

Insert paragraph

⊟Genome View[edit | edit source]

Insert paragraph

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • symbol: purD
  • product: phosphoribosylamine--glycine ligase
  • replicon: chromosome
  • strand: +
  • coordinates: 1092909..1094156
  • length: 1248
  • essential: unknown other strains

Insert paragraph

⊟Accession numbers[edit | edit source]

Insert paragraph

⊟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
    ATGAATGTATTAGTAATTGGTGCTGGTGGACGAGAACATGCACTTGCATATAAACTTAAT
    CAATCGAATCTAGTTAAACAAGTGTTTGTCATTCCAGGTAATGAGGCAATGACACCTATA
    GCTGAAGTACACACTGAAATTTCAGAACCTGATCATCAAGCGATACTAGATTTTGCTAAA
    CGGCAAAATGTTGATTGGGTAGTTATAGGTCCAGAACAGCCGCTAATTGATGGATTAGCA
    GACATTTTACGAGCGAATGGTTTCAAAGTGTTTGGTCCAAATAAGCAAGCAGCTCAAATC
    GAAGGCTCAAAATTATTTGCTAAAAAGATAATGGAAAAATATAATATTCCAACTGCTGAT
    TATAAAGAAGTTGAGCGAAAAAAGGATGCTTTAACATATATTGAAAACTGTGAATTGCCC
    GTTGTTGTCAAGAAAGATGGGTTAGCTGCTGGGAAAGGCGTTATTATTGCAGATACTATT
    GAAGCAGCCAGAAGTGCTATTGAGATTATGTATGGTGATGAAGAAGAAGGTACTGTTGTA
    TTTGAAACGTTTTTAGAAGGTGAAGAGTTCTCGCTAATGACATTTGTTAATGGTGATTTA
    GCAGTACCTTTCGACTGTATTGCACAAGATCATAAACGCGCATTTGATCATGATGAAGGA
    CCAAATACTGGTGGTATGGGGGCTTATTGTCCAGTACCACATATTAGTGACGATGTTTTA
    AAACTTACAAATGAAACAATTGCACAACCCATTGCAAAGGCAATGCTTAATGAAGGTTAT
    CAATTCTTCGGTGTATTATACATTGGTGCTATTTTAACTAAAGATGGTCCAAAAGTAATA
    GAATTTAATGCCCGTTTTGGTGATCCTGAAGCTCAAGTATTATTAAGTCGCATGGAAAGT
    GATTTAATGCAGCATATTATTGATTTAGATGAAGGAAAACGTACTGAATTCAAATGGAAA
    AATGAATCTATTGTAGGGGTCATGTTGGCATCAAAAGGATATCCTGATGCATATGAAAAA
    GGGCATAAAGTAAGTGGCTTTGATTTAAATGAAAACTATTTTGTTAGTGGATTAAAGAAG
    CAAGGTGATACCTTTGTTACTTCAGGTGGTAGAGTTATACTTGCCATCGGAAAAGGTGAC
    AATGTACAAGATGCACAGCGAGACGCATACAAAAAAGTATCACAAATACAAAGTGACCAT
    TTATTCTATCGTCATGACATTGCGAATAAAGCACTACAACTTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1248

Insert paragraph

This data comes from external databases and cannot be edited.

Insert paragraph

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1083 [new locus tag: SACOL_RS05525 ]
  • symbol: PurD
  • description: phosphoribosylamine--glycine ligase
  • length: 415
  • theoretical pI: 4.89379
  • theoretical MW: 45858.9
  • GRAVY: -0.244819

Insert paragraph

⊟Function[edit | edit source]

  • ⊞reaction:
    EC 6.3.4.13?  ExPASy
    Phosphoribosylamine--glycine ligase ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
  • ⊞TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylamine--glycine ligase (TIGR00877; EC 6.3.4.13; HMM-score: 466)
    and 11 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, large subunit (TIGR01369; EC 6.3.5.5; HMM-score: 36.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazole carboxylase, ATPase subunit (TIGR01161; EC 4.1.1.21; HMM-score: 29.2)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan D-alanine--D-alanine ligase (TIGR01205; EC 6.3.2.4; HMM-score: 28.3)
    Cellular processes Cellular processes Biosynthesis of natural products cyanophycin synthetase (TIGR02068; EC 6.3.2.29,6.3.2.30; HMM-score: 24.7)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 22.4)
    alpha-L-glutamate ligase, RimK family (TIGR00768; EC 6.3.2.-; HMM-score: 22.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylglycinamide formyltransferase 2 (TIGR01142; EC 2.1.2.-; HMM-score: 19.4)
    Metabolism Energy metabolism TCA cycle succinate-CoA ligase, beta subunit (TIGR01016; EC 6.2.1.-; HMM-score: 14.6)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 14.2)
    Metabolism Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylC (TIGR03909; HMM-score: 13.7)
    lysine biosynthesis enzyme LysX (TIGR02144; HMM-score: 13.1)
  • ⊞TheSEED  :
    • Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
    Miscellaneous Miscellaneous - no subcategory EC 6.3.4.- Ligases that form carbon-nitrogen bonds  Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
    and 1 more
    Nucleosides and Nucleotides Purines De Novo Purine Biosynthesis  Phosphoribosylamine--glycine ligase (EC 6.3.4.13)
  • ⊞PFAM:
    ATP-grasp (CL0179) GARS_A; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain (PF01071; HMM-score: 228.6)
    and 10 more
    NADP_Rossmann (CL0063) GARS_N; Phosphoribosylglycinamide synthetase, N domain (PF02844; HMM-score: 125.6)
    Hybrid (CL0105) GARS_C; Phosphoribosylglycinamide synthetase, C domain (PF02843; HMM-score: 86.6)
    ATP-grasp (CL0179) ATP-grasp_3; ATP-grasp domain (PF02655; HMM-score: 29.8)
    ATP-grasp; ATP-grasp domain (PF02222; HMM-score: 24.6)
    RimK; RimK-like ATP-grasp domain (PF08443; HMM-score: 17.5)
    ATP-grasp_5; ATP-grasp domain (PF13549; HMM-score: 16.7)
    Dala_Dala_lig_C; D-ala D-ala ligase C-terminus (PF07478; HMM-score: 16.6)
    CPSase_L_D2; Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786; HMM-score: 15.9)
    MurF-HprK_N (CL0365) Mur_ligase; Mur ligase family, catalytic domain (PF01225; HMM-score: 15.8)
    ATP-grasp (CL0179) ATP-grasp_2; ATP-grasp domain (PF08442; HMM-score: 13.6)

Insert paragraph

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

  • domains:
  • modifications:
  • cofactors: Mg2+, Mn2+
  • effectors:

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⊟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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9929
    • Cytoplasmic Membrane Score: 0.0005
    • Cell wall & surface Score: 0.0003
    • Extracellular Score: 0.0063
  • ⊞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): 0.008564
    • TAT(Tat/SPI): 0.000596
    • LIPO(Sec/SPII): 0.001631
  • predicted transmembrane helices (TMHMM): 0

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⊟Accession numbers[edit | edit source]

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⊟Protein sequence[edit | edit source]

  • MNVLVIGAGGREHALAYKLNQSNLVKQVFVIPGNEAMTPIAEVHTEISEPDHQAILDFAKRQNVDWVVIGPEQPLIDGLADILRANGFKVFGPNKQAAQIEGSKLFAKKIMEKYNIPTADYKEVERKKDALTYIENCELPVVVKKDGLAAGKGVIIADTIEAARSAIEIMYGDEEEGTVVFETFLEGEEFSLMTFVNGDLAVPFDCIAQDHKRAFDHDEGPNTGGMGAYCPVPHISDDVLKLTNETIAQPIAKAMLNEGYQFFGVLYIGAILTKDGPKVIEFNARFGDPEAQVLLSRMESDLMQHIIDLDEGKRTEFKWKNESIVGVMLASKGYPDAYEKGHKVSGFDLNENYFVSGLKKQGDTFVTSGGRVILAIGKGDNVQDAQRDAYKKVSQIQSDHLFYRHDIANKALQLK

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⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1731 [5]
  • ⊟interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [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)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL1753universal stress protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

  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 6.17 6.18 6.19 6.20 6.21 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)
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⊟Expression & Regulation[edit | edit source]

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⊟Operon[edit | edit source]

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⊟Regulation[edit | edit source]

  • data available for N315

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⊟Transcription pattern[edit | edit source]

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

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⊟Protein stability[edit | edit source]

  • half-life: 25.44 h [1]

  1. ↑ 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)
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⊞Biological Material[edit | edit source]

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

⊞Other Information[edit | edit source]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

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⊟Relevant publications[edit | edit source]

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