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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0439 [new locus tag: SACOL_RS02210 ]
- pan locus tag?: SAUPAN001916000
- symbol: rpsR
- pan gene symbol?: rpsR
- synonym:
- product: 30S ribosomal protein S18
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0439 [new locus tag: SACOL_RS02210 ]
- symbol: rpsR
- product: 30S ribosomal protein S18
- replicon: chromosome
- strand: +
- coordinates: 443566..443808
- length: 243
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236498 NCBI
- RefSeq: YP_185330 NCBI
- BioCyc: see SACOL_RS02210
- MicrobesOnline: 911909 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
61
121
181
241ATGGCAGGTGGACCAAGAAGAGGCGGACGTCGTCGTAAAAAAGTATGCTATTTCACAGCA
AATGGTATTACACATATCGACTACAAAGACACTGAATTATTAAAACGTTTTATCTCAGAA
CGCGGTAAAATTTTACCACGTCGTGTAACTGGTACTTCAGCTAAATATCAACGTATGTTG
ACTACAGCTATCAAACGTTCTCGTCATATGGCATTATTACCATATGTTAAAGAAGAACAA
TAA60
120
180
240
243
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0439 [new locus tag: SACOL_RS02210 ]
- symbol: RpsR
- description: 30S ribosomal protein S18
- length: 80
- theoretical pI: 11.5763
- theoretical MW: 9309.89
- GRAVY: -0.78125
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bS18 (TIGR00165; HMM-score: 126.6)
- TheSEED :
- SSU ribosomal protein S18p
- SSU ribosomal protein S18p, zinc-independent
Phages, Prophages, Transposable elements, Plasmids Pathogenicity islands Staphylococcal pathogenicity islands SaPI SSU ribosomal protein S18pand 1 more - PFAM: no clan defined Ribosomal_S18; Ribosomal protein S18 (PF01084; HMM-score: 98.9)
⊟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): 0.009082
- TAT(Tat/SPI): 0.006745
- LIPO(Sec/SPII): 0.00536
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MAGGPRRGGRRRKKVCYFTANGITHIDYKDTELLKRFISERGKILPRRVTGTSAKYQRMLTTAIKRSRHMALLPYVKEEQ
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 731 [4]
- interaction partners:
SACOL0842 (eno) phosphopyruvate hydratase [5] (data from MRSA252) SACOL1198 (ftsA) cell division protein FtsA [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [5] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [5] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [5] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [5] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [5] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [5] (data from MRSA252) SACOL0015 (rplI) 50S ribosomal protein L9 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [5] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [5] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [5] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [5] (data from MRSA252) SACOL2212 (rplQ) 50S ribosomal protein L17 [5] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [5] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [5] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [5] (data from MRSA252) SACOL2228 (rplX) 50S ribosomal protein L24 [5] (data from MRSA252) SACOL1700 (rpmA) 50S ribosomal protein L27 [5] (data from MRSA252) SACOL2231 (rpmC) 50S ribosomal protein L29 [5] (data from MRSA252) SACOL2112 (rpmE2) 50S ribosomal protein L31 [5] (data from MRSA252) SACOL1726 (rpmI) 50S ribosomal protein L35 [5] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [5] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [5] (data from MRSA252) SACOL0592 (rpsG) 30S ribosomal protein S7 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL2240 (rpsJ) 30S ribosomal protein S10 [5] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [5] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [5] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [5] (data from MRSA252) SACOL1292 (rpsO) 30S ribosomal protein S15 [5] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [5] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [5] (data from MRSA252) SACOL1642 (rpsT) 30S ribosomal protein S20 [5] (data from MRSA252) SACOL0303 5'-nucleotidase [5] (data from MRSA252) SACOL0552 hypothetical protein [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0742 hypothetical protein [5] (data from MRSA252) SACOL1294 metallo-beta-lactamase [5] (data from MRSA252) SACOL1651 hypothetical protein [5] (data from MRSA252) SACOL1753 universal stress protein [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: rpsF > ssb2 > rpsR
⊟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: 7.66 h [6]
⊟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, 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) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 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) - ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)