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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00284
- pan locus tag?: SAUPAN001228000
- symbol: SAOUHSC_00284
- pan gene symbol?: —
- synonym:
- product: 5'-nucleotidase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00284
- symbol: SAOUHSC_00284
- product: 5'-nucleotidase
- replicon: chromosome
- strand: +
- coordinates: 299299..300189
- length: 891
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3918967 NCBI
- RefSeq: YP_498875 NCBI
- BioCyc: G1I0R-263 BioCyc
- MicrobesOnline: 1288769 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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841ATGAATAAAATTTCAAAGTATATTGCAATAGCATCATTATCGGTAGCGGTTACAGTTTCA
GCACCACAAACGACAAATTCTACAGCGTTTGCCAAAAGTTCTGCTGAAGTTCAACAAACG
CAACAAGCTTCTATACCAGCATCACAAAAGGCGAATCTTGGTAATCAAAATATTATGGCA
GTGGCTTGGTATCAAAATTCAGCTGAAGCAAAAGCATTATATTTACAAGGTTATAACAGT
GCAAAGACACAGTTAGATAAAGAGATTAAAAAGAATAAAGGTAAACATAAGTTAGCTATT
GCTTTGGATTTAGATGAAACAGTTTTAGATAATTCTCCATATCAAGGCTATGCATCAATA
CATAATAAACCTTTCCCAGAAGGTTGGCATGAATGGGTACAAGCTGCTAAAGCTAAACCT
GTCTATGGCGCAAAAGAATTCTTGAAATATGCTGACAAAAAAGGTGTCGATATCTACTAT
ATTTCTGATAGAGATAAAGAAAAAGATTTAAAGGCAACACAAAAGAACTTAAAACAACAA
GGTATCCCTCAAGCTAAGAAGAGTCATATTTTACTAAAAGGTAAAGATGATAAGAGTAAA
GAATCACGCAGACAAATGGTTCAAAAGGATCATAAACTTGTCATGCTATTTGGAGATAAT
TTATTAGACTTTACAGATCCAAAAGAAGCTACAGCTGAATCTCGTGAAGCATTAATTGAA
AAACATAAAGACGATTTCGGTAAGAAATATATCATTTTCCCTAACCCAATGTATGGTAGT
TGGGAAGCTACGATTTACAACAATAACTATAAAGCAAGTGACAAAGCAAAAGATAAATTA
CGTAAAAATGCTATTAAGCAATTCGATCCTAAAACAGGCGAAGTTAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00284
- symbol: SAOUHSC_00284
- description: 5'-nucleotidase
- length: 296
- theoretical pI: 10.0788
- theoretical MW: 33351.7
- GRAVY: -0.8125
⊟Function[edit | edit source]
- TIGRFAM: Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides 5'-nucleotidase, lipoprotein e(P4) family (TIGR01533; HMM-score: 399.1)Transport and binding proteins Other 5'-nucleotidase, lipoprotein e(P4) family (TIGR01533; HMM-score: 399.1)and 3 moreplant acid phosphatase (TIGR01675; HMM-score: 41.3)HAD phosphatase, family IIIB (TIGR01672; EC 3.1.3.-; HMM-score: 17.9)colanic acid biosynthesis glycosyltransferase WcaE (TIGR04009; EC 2.4.-.-; HMM-score: 15.5)
- TheSEED :
- Acid phosphatase (EC 3.1.3.2)
- PFAM: HAD (CL0137) Acid_phosphat_B; HAD superfamily, subfamily IIIB (Acid phosphatase) (PF03767; HMM-score: 185.7)and 1 moreHydrolase_6; haloacid dehalogenase-like hydrolase (PF13344; HMM-score: 17.9)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: unknown (no significant prediction)
- Cytoplasmic Score: 0
- Cytoplasmic Membrane Score: 3.33
- Cellwall Score: 3.33
- Extracellular Score: 3.33
- Internal Helices: 0
- LocateP: Secretory(released) (with CS)
- Prediction by SwissProt Classification: Extracellular
- Pathway Prediction: Sec-(SPI)
- Intracellular possibility: -0.17
- Signal peptide possibility: 1
- N-terminally Anchored Score: -1
- Predicted Cleavage Site: NSTAFAKS
- SignalP: Signal peptide SP(Sec/SPI) length 31 aa
- SP(Sec/SPI): 0.955558
- TAT(Tat/SPI): 0.021208
- LIPO(Sec/SPII): 0.015906
- Cleavage Site: CS pos: 31-32. AFA-KS. Pr: 0.6720
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MNKISKYIAIASLSVAVTVSAPQTTNSTAFAKSSAEVQQTQQASIPASQKANLGNQNIMAVAWYQNSAEAKALYLQGYNSAKTQLDKEIKKNKGKHKLAIALDLDETVLDNSPYQGYASIHNKPFPEGWHEWVQAAKAKPVYGAKEFLKYADKKGVDIYYISDRDKEKDLKATQKNLKQQGIPQAKKSHILLKGKDDKSKESRRQMVQKDHKLVMLFGDNLLDFTDPKEATAESREALIEKHKDDFGKKYIIFPNPMYGSWEATIYNNNYKASDKAKDKLRKNAIKQFDPKTGEVK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell:
- interaction partners:
SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [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_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [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_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02505 (rplP) 50S ribosomal protein L16 [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_01755 (rpmA) 50S ribosomal protein L27 [3] (data from MRSA252) SAOUHSC_00524 (rpoB) DNA-directed RNA polymerase subunit beta [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_01250 (rpsO) 30S ribosomal protein S15 [3] (data from MRSA252) SAOUHSC_01208 (rpsP) 30S ribosomal protein S16 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [3] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [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_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00921 3-oxoacyl- synthase [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [3] (data from MRSA252) SAOUHSC_01035 hypothetical protein [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [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_01287 glutamine synthetase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01698 hypothetical protein [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01854 hypothetical protein [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [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_02869 1-pyrroline-5-carboxylate dehydrogenase [3] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02968 ornithine carbamoyltransferase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟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]
- 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]
- ↑ 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 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 3.62 3.63 3.64 3.65 3.66 3.67 3.68 3.69 3.70 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) - ↑ 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)