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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1976 [new locus tag: SACOL_RS10330 ]
- pan locus tag?: SAUPAN004947000
- symbol: SACOL1976
- pan gene symbol?: nos
- synonym:
- product: nitric-oxide synthase, oxygenase subunit
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1976 [new locus tag: SACOL_RS10330 ]
- symbol: SACOL1976
- product: nitric-oxide synthase, oxygenase subunit
- replicon: chromosome
- strand: +
- coordinates: 2039628..2040704
- length: 1077
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238410 NCBI
- RefSeq: YP_186800 NCBI
- BioCyc: see SACOL_RS10330
- MicrobesOnline: 913454 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1021ATGTTATTTAAAGAGGCTCAAGCTTTCATAGAAAACATGTATAAAGAGTGTCATTATGAA
ACGCAAATTATCAATAAACGTTTACATGACATTGAACTAGAAATAAAAGAAACTGGGACA
TATACACATACAGAAGAAGAACTTATTTATGGTGCTAAAATGGCTTGGCGTAATTCAAAT
CGTTGCATTGGTCGTTTATTTTGGGATTCGTTAAATGTCATTGATGCAAGAGATGTTACT
GACGAAGCATCGTTCTTATCATCAATTACTTATCATATTACACAGGCTACAAATGAAGGT
AAATTAAAGCCGTATATTACTATATATGCTCCAAAGGATGGACCTAAAATTTTCAACAAT
CAATTAATTCGCTATGCTGGCTATGACAATTGTGGTGATCCTGCTGAAAAAGAAGTTACA
CGCTTAGCAAATCACTTAGGTTGGAAAGGAAAAGGTACTAATTTTGACGTGTTACCACTG
ATTTACCAATTACCTAATGAGTCAGTTAAATTTTACGAATATCCTACTTCATTAATTAAA
GAAGTACCTATTGAACATAATCATTATCCAAAATTAAGAAAATTGAACTTAAAATGGTAT
GCAGTCCCTATCATTTCCAATATGGACTTAAAAATCGGTGGCATTGTATATCCAACTGCA
CCCTTTAACGGTTGGTATATGGTAACTGAAATTGGCGTACGTAACTTTATTGATGATTAC
CGTTACAATTTACTAGAAAAAGTTGCAGATGCGTTTGAATTTGATACACTTAAAAATAAT
TCATTTAATAAAGATCGAGCACTTGTTGAATTGAACTATGCTGTGTATCATTCCTTTAAA
AAAGAAGGCGTATCAATTGTCGATCATTTGACCGCTGCAAAGCAATTCGAACTATTCGAA
CGTAACGAAGCACAACAAGGTCGTCAAGTTACCGGAAAATGGTCTTGGCTAGCACCGCCA
TTATCTCCAACATTGACGTCAAATTATCATCACGGATATGACAATACAGTAAAAGATCCA
AACTTTTTCTATAAAAAGAAAGAATCAAATGCTAACCAGTGCCCTTTCCATCATTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1976 [new locus tag: SACOL_RS10330 ]
- symbol: SACOL1976
- description: nitric-oxide synthase, oxygenase subunit
- length: 358
- theoretical pI: 7.00032
- theoretical MW: 41709.9
- GRAVY: -0.563966
⊟Function[edit | edit source]
- reaction: EC 1.14.14.47? ExPASyNitric-oxide synthase (flavodoxin) 2 L-arginine + 3 reduced flavodoxin + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
- TIGRFAM:
- TheSEED :
- Nitric-oxide synthase (flavodoxin) (EC 1.14.14.47)
- PFAM: no clan defined NO_synthase; Nitric oxide synthase, oxygenase domain (PF02898; HMM-score: 506)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: (6S)-5,6,7,8-tetrahydrofolate, heme
- 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): 0.004813
- TAT(Tat/SPI): 0.000432
- LIPO(Sec/SPII): 0.000773
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MLFKEAQAFIENMYKECHYETQIINKRLHDIELEIKETGTYTHTEEELIYGAKMAWRNSNRCIGRLFWDSLNVIDARDVTDEASFLSSITYHITQATNEGKLKPYITIYAPKDGPKIFNNQLIRYAGYDNCGDPAEKEVTRLANHLGWKGKGTNFDVLPLIYQLPNESVKFYEYPTSLIKEVPIEHNHYPKLRKLNLKWYAVPIISNMDLKIGGIVYPTAPFNGWYMVTEIGVRNFIDDYRYNLLEKVADAFEFDTLKNNSFNKDRALVELNYAVYHSFKKEGVSIVDHLTAAKQFELFERNEAQQGRQVTGKWSWLAPPLSPTLTSNYHHGYDNTVKDPNFFYKKKESNANQCPFHH
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4]
- quantitative data / protein copy number per cell: 76 [5]
- interaction partners:
SACOL0842 (eno) phosphopyruvate hydratase [6] (data from MRSA252) SACOL1245 (fabG1) 3-oxoacyl-ACP reductase [6] (data from MRSA252) SACOL0593 (fusA) elongation factor G [6] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [6] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [6] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [6] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [6] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [6] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [6] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [6] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [6] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [6] (data from MRSA252) SACOL2104 (upp) uracil phosphoribosyltransferase [6] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟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: 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]
- ↑ 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, 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) - ↑ 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) - ↑ 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 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]
François J M Chartier, Sébastien P Blais, Manon Couture
A weak Fe-O bond in the oxygenated complex of the nitric-oxide synthase of Staphylococcus aureus.
J Biol Chem: 2006, 281(15);9953-62
[PubMed:16473878] [WorldCat.org] [DOI] (P p)