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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1759 [new locus tag: SACOL_RS08995 ]
- pan locus tag?: SAUPAN004362000
- symbol: SACOL1759
- pan gene symbol?: uspA1
- synonym:
- product: universal stress protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1759 [new locus tag: SACOL_RS08995 ]
- symbol: SACOL1759
- product: universal stress protein
- replicon: chromosome
- strand: +
- coordinates: 1798751..1799251
- length: 501
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3235995 NCBI
- RefSeq: YP_186593 NCBI
- BioCyc: see SACOL_RS08995
- MicrobesOnline: 913204 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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481ATGATTACTTACAAAAATATTTTAATCGCAGTTGACGGTTCACATGAAGCGGAATGGGCA
TTTAACAGAGCAGTTGGTGTTGCTAAACGTAACGATGCGAAGTTAACAATTGTGAATGTA
ATTGATTCAAGAACGTATTCTTCTTATGAAGTTTATGATGCTCAATTTACTGAAAAATCT
AAGCATTTTGCAGAAGAATTATTAAATGGTTATAAAGAAGTAGCTACTAACGCTGGTGTT
AAAGATGTAGAAACGCGTCTAGAGTTTGGCTCTCCTAAATCTATCATTCCTAAAAAGCTT
GCACATGAAATTAATGCAGACTTGATTATGAGTGGTACATCAGGCTTAAATGCCGTGGAA
AGATTTATTGTTGGTTCTGTATCAGAATCTATCGTTCGTCATGCGCCATGTGACGTGTTA
GTTGTTCGTACTGAAGAGTTACCAGCAGACTTCCAACCACAAGTTGCAACAACTCAATTA
CGTGAAAAATATCAAAATTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1759 [new locus tag: SACOL_RS08995 ]
- symbol: SACOL1759
- description: universal stress protein
- length: 166
- theoretical pI: 5.67748
- theoretical MW: 18474.7
- GRAVY: -0.259639
⊟Function[edit | edit source]
- TIGRFAM: DNA metabolism DNA replication, recombination, and repair deoxyribodipyrimidine photolyase (TIGR00591; EC 4.1.99.3; HMM-score: 16.1)
- TheSEED :
- Universal stress protein family
- PFAM: HUP (CL0039) Usp; Universal stress protein family (PF00582; HMM-score: 123.4)and 1 moreno clan defined DUF693; Protein of unknown function (DUF693) (PF05113; HMM-score: 14.5)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- 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): 0.008849
- TAT(Tat/SPI): 0.000553
- LIPO(Sec/SPII): 0.001624
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MITYKNILIAVDGSHEAEWAFNRAVGVAKRNDAKLTIVNVIDSRTYSSYEVYDAQFTEKSKHFAEELLNGYKEVATNAGVKDVETRLEFGSPKSIIPKKLAHEINADLIMSGTSGLNAVERFIVGSVSESIVRHAPCDVLVVRTEELPADFQPQVATTQLREKYQN
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4]
- quantitative data / protein copy number per cell: 4776 [5]
- interaction partners:
SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [6] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [6] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [6] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [6] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [6] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [6] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [6] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [6] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [6] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [6] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [6] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [6] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [6] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [6] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [6] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [6] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [6] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [6] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [6] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [6] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [6] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [6] (data from MRSA252) SACOL0944 NADH dehydrogenase [6] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [6] (data from MRSA252) SACOL2173 alkaline shock protein 23 [6] (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: data available for NCTC8325
⊟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]
- ↑ 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 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 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)