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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
- pan locus tag?: SAUPAN002234000
- symbol: purR
- pan gene symbol?: purR
- synonym:
- product: pur operon repressor
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
- symbol: purR
- product: pur operon repressor
- replicon: chromosome
- strand: +
- coordinates: 547963..548787
- length: 825
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237114 NCBI
- RefSeq: YP_185427 NCBI
- BioCyc: see SACOL_RS02755
- MicrobesOnline: 912011 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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781ATGAGATATAAACGAAGCGAGAGAATTGTTTTTATGACGCAATATTTGATGAACCATCCG
AATAAATTGATTCCATTAACTTTTTTTGTGAAAAAATTTAAACAGGCGAAGTCTTCAATA
AGTGAAGATGTCCAAATTATAAAAAATACATTCCAAAAAGAAAAGTTAGGTACAGTAATT
ACTACTGCTGGCGCAAGTGGTGGTGTTACGTATAAACCAATGATGAGTAAAGAAGAGGCG
ACTGAAGTTGTTAATGAGGTCATTACTCTATTAGAAGAGAAAGAACGTTTGTTACCTGGC
GGATATTTATTTTTATCAGATTTGGTAGGTAATCCATCGCTACTAAACAAAGTTGGTAAG
TTAATTGCCAGTATTTACATGGAAGAAAAATTAGATGCTGTTGTTACCATTGCGACAAAA
GGTATTTCATTGGCAAATGCGGTTGCTAATATTTTAAATTTACCAGTAGTAGTGATTAGA
AAAGACAACAAGGTGACTGAAGGTTCTACAGTTTCAATTAATTACGTTTCAGGATCTTCA
AGAAAAATAGAAACAATGGTACTTTCGAAGAGAACTTTAGCAGAAAATTCAAATGTTTTA
GTTGTCGATGATTTTATGAGGGCTGGTGGCTCTATTAATGGTGTTATGAATTTAATGAAT
GAGTTTAAAGCCCATGTAAAAGGGGTATCAGTACTTGTAGAATCAAAAGAAGTTAAACAA
AGATTGATTGAAGATTATACTTCCTTAGTGAAATTATCTGATGTAGATGAATATAATCAA
GAGTTTAACGTAGAACCTGGCAACAGTTTATCTAAGTTTTCATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
- symbol: PurR
- description: pur operon repressor
- length: 274
- theoretical pI: 9.54206
- theoretical MW: 30395.1
- GRAVY: -0.0715328
⊟Function[edit | edit source]
- TIGRFAM: Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis pur operon repressor PurR (TIGR01743; HMM-score: 361.7)Regulatory functions DNA interactions pur operon repressor PurR (TIGR01743; HMM-score: 361.7)and 6 morePurines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides xanthine phosphoribosyltransferase (TIGR01744; EC 2.4.2.22; HMM-score: 67)Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides adenine phosphoribosyltransferase (TIGR01090; EC 2.4.2.7; HMM-score: 65.1)Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR00336; EC 2.4.2.10; HMM-score: 43.2)Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR01367; EC 2.4.2.10; HMM-score: 30.3)Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis ribose-phosphate diphosphokinase (TIGR01251; EC 2.7.6.1; HMM-score: 20)Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides hypoxanthine phosphoribosyltransferase (TIGR01203; EC 2.4.2.8; HMM-score: 18.1)
- TheSEED :
- Pur operon repressor PurR
- PFAM: HTH (CL0123) PuR_N; Bacterial purine repressor, N-terminal (PF09182; HMM-score: 107.4)and 1 morePRTase-like (CL0533) Pribosyltran; Phosphoribosyl transferase domain (PF00156; HMM-score: 76.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
- genes regulated by PurR, TF important in Purine metabolism: in N315
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 0.67
- Signal peptide possibility: -0.5
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.040109
- TAT(Tat/SPI): 0.000536
- LIPO(Sec/SPII): 0.001557
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MRYKRSERIVFMTQYLMNHPNKLIPLTFFVKKFKQAKSSISEDVQIIKNTFQKEKLGTVITTAGASGGVTYKPMMSKEEATEVVNEVITLLEEKERLLPGGYLFLSDLVGNPSLLNKVGKLIASIYMEEKLDAVVTIATKGISLANAVANILNLPVVVIRKDNKVTEGSTVSINYVSGSSRKIETMVLSKRTLAENSNVLVVDDFMRAGGSINGVMNLMNEFKAHVKGVSVLVESKEVKQRLIEDYTSLVKLSDVDEYNQEFNVEPGNSLSKFS
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Signal peptide containing [1] [2] [3]
- quantitative data / protein copy number per cell: 537 [4]
- interaction partners:
SACOL1215 (carB) carbamoyl phosphate synthase large subunit [5] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [5] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [5] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [5] (data from MRSA252) SACOL0460 (guaB) inosine-5'-monophosphate dehydrogenase [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [5] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: ipk > purR > SACOL0540
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: 208.27 h [6]
⊟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]
- ↑ 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) - ↑ 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) - ↑ 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) - ↑ 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) - ↑ 5.00 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 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) - ↑ 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)