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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01658
- pan locus tag?: SAUPAN004138000
- symbol: SAOUHSC_01658
- pan gene symbol?: nfo
- synonym:
- product: endonuclease IV
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01658
- symbol: SAOUHSC_01658
- product: endonuclease IV
- replicon: chromosome
- strand: -
- coordinates: 1570227..1571117
- length: 891
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3920109 NCBI
- RefSeq: YP_500169 NCBI
- BioCyc: G1I0R-1541 BioCyc
- MicrobesOnline: 1290083 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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841ATGTTATTAGGATCACATGTTTCAATGAGTGGTAAAAAGATGTTAGAAGGTTCTGCTATA
GAAGCGCATGAATATGGTGAAACAACATTTATGATTTATACTGGTGCACCTCAAAACACG
CGCCGTAAAAGTATTGAAGATTTAAATATAACTAAAGGTCATGAAGTGATGGAAAAATAT
GGTTTATCTAATATTGTTGTTCATGCACCATACATCATTAATATTGCAAATACAACCAAA
CCAGAAACGTTTAATCTTGGTGTAGATTTCTTGCAACAAGAAATTGAAAGAACGCAAGCT
ATAGGGGCTAAAGATATTGTATTACATCCAGGTGCGCATGTTGGAGCTGGTGTTGATGCC
GGAATTAATAAGATTATTGAAGGATTAAATGAAGTTTTAACGAATGACAATAATGTACGT
ATTGCGCTTGAAACGATGGCAGGTAAAGGTACAGAGATTGGTCGCTCATTTGAAGAGTTA
GCACGTATTATTGATGGAGTTCATAATAACGAACGTTTATCAGTATGTTTTGATACATGT
CATACGCATGATGCTGGATATAATGTTAAAGAGGACTTTGATGGCGTATTAAATGAATTT
GATAAAATCATTGGAGTCGACAGAATCAAAGTTGTTCATGTCAATGATTCTAAAAATGAC
CGTGGCGCTCAAAAAGACCGACATGAAAATATTGGCTTCGGTTACATTGGTTTTGATGCA
TTAAATTACATTGTGCATCATGATAGTTTTAAAGATATTCCGAAAATCTTAGAAACACCT
TATGTTGGTGAAGATAAGAAAAATAAAAAACCGCCATATAAACTTGAAATTGAAATGTTA
AAACAACAGCAATTTGACCCAGAATTAAAAAATAAGGTTATGCAACAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01658
- symbol: SAOUHSC_01658
- description: endonuclease IV
- length: 296
- theoretical pI: 5.89598
- theoretical MW: 33158.3
- GRAVY: -0.471284
⊟Function[edit | edit source]
- reaction: EC 3.1.21.2? ExPASyDeoxyribonuclease IV Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products
- TIGRFAM: DNA metabolism DNA replication, recombination, and repair apurinic endonuclease (APN1) (TIGR00587; HMM-score: 331.8)
- TheSEED :
- Endonuclease IV (EC 3.1.21.2)
- PFAM: TIM_barrel (CL0036) AP_endonuc_2; Xylose isomerase-like TIM barrel (PF01261; HMM-score: 131.9)and 3 moreno clan defined UDG; Uracil DNA glycosylase superfamily (PF03167; HMM-score: 19.3)TFIIA_gamma_N; Transcription initiation factor IIA, gamma subunit, helical domain (PF02268; HMM-score: 12.6)DASH_Dad1; DASH complex subunit Dad1 (PF08649; HMM-score: 11.5)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Zn2+
- 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): 0.010717
- TAT(Tat/SPI): 0.000764
- LIPO(Sec/SPII): 0.001682
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MLLGSHVSMSGKKMLEGSAIEAHEYGETTFMIYTGAPQNTRRKSIEDLNITKGHEVMEKYGLSNIVVHAPYIINIANTTKPETFNLGVDFLQQEIERTQAIGAKDIVLHPGAHVGAGVDAGINKIIEGLNEVLTNDNNVRIALETMAGKGTEIGRSFEELARIIDGVHNNERLSVCFDTCHTHDAGYNVKEDFDGVLNEFDKIIGVDRIKVVHVNDSKNDRGAQKDRHENIGFGYIGFDALNYIVHHDSFKDIPKILETPYVGEDKKNKKPPYKLEIEMLKQQQFDPELKNKVMQQ
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00767 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01845 formate--tetrahydrofolate ligase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_01655 < SAOUHSC_01656 < SAOUHSC_01657 < SAOUHSC_01658 < SAOUHSC_01659predicted SigA promoter [4] : SAOUHSC_01655 < SAOUHSC_01656 < SAOUHSC_01657 < S654 < SAOUHSC_01658 < SAOUHSC_01659predicted SigA promoter [4] : SAOUHSC_01655 < SAOUHSC_01656 < SAOUHSC_01657 < S654 < SAOUHSC_01658 < SAOUHSC_01659 < S655 < SAOUHSC_01660 < SAOUHSC_01661 < SAOUHSC_01662 < S656 < SAOUHSC_01663
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟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]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 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) - ↑ 4.0 4.1 4.2 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)