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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00483
- pan locus tag?: SAUPAN002249000
- symbol: SAOUHSC_00483
- pan gene symbol?: —
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00483
- symbol: SAOUHSC_00483
- product: hypothetical protein
- replicon: chromosome
- strand: +
- coordinates: 480715..481116
- length: 402
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3920341 NCBI
- RefSeq: YP_499060 NCBI
- BioCyc: G1I0R-447 BioCyc
- MicrobesOnline: 1288958 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
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361ATGTCAATCGAAGTTGGAAATAAGCTTAAAGGTAAAGTCACTGGTATTAAAAAGTTTGGT
GCATTCGTAGAATTACCTGAAGGAAAAAGTGGTTTAGTTCACATTAGTGAAGTCGCAGAT
AATTATGTTGAAAACGTAGAAGAGCACCTTTCTGTTGGTGATGAAGTAGACGTAAAAGTA
TTATCTATTGCTGATGATGGAAAAATTAGTCTTTCAATTAAGAAAGCTAAAGACCGTCCA
CGTAGACAACATACGAGTAAACCAAGTCATCAAAAACCAGTGCAAAAAGCCGAAGATTTT
GAAAAGAAATTAAGCAATTTCTTAAAAGATAGTGAAGATAAATTAACTTCAATCAAACGT
CAAACAGAATCTAGACGCGGTGGCAAAGGTTCAAGACGTTAA60
120
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402
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00483
- symbol: SAOUHSC_00483
- description: hypothetical protein
- length: 133
- theoretical pI: 10.3587
- theoretical MW: 14811.7
- GRAVY: -0.873684
⊟Function[edit | edit source]
- TIGRFAM: Transcription Degradation of RNA polyribonucleotide nucleotidyltransferase (TIGR03591; EC 2.7.7.8; HMM-score: 75.4)Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bS1 (TIGR00717; HMM-score: 69.5)and 7 moreguanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase (TIGR02696; EC 2.7.-.-,2.7.7.8; HMM-score: 47.4)Transcription Degradation of RNA ribonuclease R (TIGR02063; EC 3.1.-.-; HMM-score: 36.6)Transcription Degradation of RNA VacB and RNase II family 3'-5' exoribonucleases (TIGR00358; EC 3.1.13.1; HMM-score: 24.2)Transcription Degradation of RNA ribonuclease, Rne/Rng family (TIGR00757; EC 3.1.4.-; HMM-score: 18.6)Transcription DNA-dependent RNA polymerase DNA-directed RNA polymerase (TIGR00448; EC 2.7.7.6; HMM-score: 18.3)Energy metabolism Glycolysis/gluconeogenesis carbon storage regulator (TIGR00202; HMM-score: 14.2)Regulatory functions RNA interactions carbon storage regulator (TIGR00202; HMM-score: 14.2)
- TheSEED :
- RNA binding protein, contains ribosomal protein S1 domain
- PFAM: OB (CL0021) S1; S1 RNA binding domain (PF00575; HMM-score: 74.6)and 2 moreS1_2; S1 domain (PF13509; HMM-score: 14.2)no clan defined CsrA; Global regulator protein family (PF02599; HMM-score: 12.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟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: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.002975
- TAT(Tat/SPI): 0.000161
- LIPO(Sec/SPII): 0.000482
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MSIEVGNKLKGKVTGIKKFGAFVELPEGKSGLVHISEVADNYVENVEEHLSVGDEVDVKVLSIADDGKISLSIKKAKDRPRRQHTSKPSHQKPVQKAEDFEKKLSNFLKDSEDKLTSIKRQTESRRGGKGSRR
⊟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_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_00520 (rplJ) 50S ribosomal protein L10 [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_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_01250 (rpsO) 30S ribosomal protein S15 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02608 hypothetical protein [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_00474 > SAOUHSC_00475 > SAOUHSC_00477 > SAOUHSC_00479 > SAOUHSC_00480 > SAOUHSC_00481 > SAOUHSC_00482 > SAOUHSC_00483predicted SigA promoter [4] : S158 > SAOUHSC_00475 > SAOUHSC_00477 > SAOUHSC_00479 > SAOUHSC_00480 > SAOUHSC_00481 > SAOUHSC_00482 > SAOUHSC_00483 > S159 > SAOUHSC_00484
⊟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 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)