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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0592 [new locus tag: SACOL_RS03070 ]
- pan locus tag?: SAUPAN002318000
- symbol: rpsG
- pan gene symbol?: rpsG
- synonym:
- product: 30S ribosomal protein S7
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0592 [new locus tag: SACOL_RS03070 ]
- symbol: rpsG
- product: 30S ribosomal protein S7
- replicon: chromosome
- strand: +
- coordinates: 615267..615737
- length: 471
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236182 NCBI
- RefSeq: YP_185478 NCBI
- BioCyc:
- MicrobesOnline: 912072 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
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421ATGCCTCGTAAAGGATCAGTACCTAAAAGAGACGTATTACCAGATCCAATTCATAACTCT
AAGTTAGTAACTAAATTAATTAACAAAATTATGTTAGATGGTAAACGTGGAACAGCACAA
AGAATTCTTTATTCAGCATTCGACCTAGTTGAACAACGCAGTGGTCGTGATGCATTAGAA
GTATTCGAAGAAGCAATCAACAACATTATGCCAGTATTAGAAGTTAAAGCTCGTCGCGTA
GGTGGTTCTAACTATCAAGTACCAGTAGAAGTTCGTCCAGAGCGTCGTACTACTTTAGGT
TTACGTTGGTTAGTTAACTATGCACGTCTTCGTGGTGAAAAAACGATGGAAGATCGTTTA
GCTAACGAAATTTTAGATGCAGCAAATAATACAGGTGGTGCCGTTAAGAAACGTGAGGAC
ACTCACAAAATGGCTGAAGCAAACAAAGCATTTGCTCACTACCGTTGGTAA60
120
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471
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0592 [new locus tag: SACOL_RS03070 ]
- symbol: RpsG
- description: 30S ribosomal protein S7
- length: 156
- theoretical pI: 10.6134
- theoretical MW: 17794.4
- GRAVY: -0.622436
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS7 (TIGR01029; HMM-score: 230.3)and 1 moreProtein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS7 (TIGR01028; HMM-score: 66)
- TheSEED: and 2 more
- PFAM: no clan defined Ribosomal_S7; Ribosomal protein S7p/S5e (PF00177; HMM-score: 224.5)and 1 moreCheC-like (CL0355) CheX; Chemotaxis phosphatase CheX (PF13690; HMM-score: 13)
⊟Structure, modifications & interactions[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
- protein partners:
SACOL0842 (eno) phosphopyruvate hydratase [1] (data from MRSA252) SACOL1198 (ftsA) cell division protein FtsA [1] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [1] (data from MRSA252) SACOL0173 (ipdC) indole-3-pyruvate decarboxylase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [1] (data from MRSA252) SACOL1011 (ppnK) inorganic polyphosphate/ATP-NAD kinase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [1] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [1] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [1] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [1] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [1] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [1] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [1] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [1] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [1] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [1] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [1] (data from MRSA252) SACOL1238 (rpmB) 50S ribosomal protein L28 [1] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [1] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [1] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [1] (data from MRSA252) SACOL2240 (rpsJ) 30S ribosomal protein S10 [1] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [1] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [1] (data from MRSA252) SACOL1292 (rpsO) 30S ribosomal protein S15 [1] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [1] (data from MRSA252) SACOL0439 (rpsR) 30S ribosomal protein S18 [1] (data from MRSA252) SACOL0816 (secA) preprotein translocase subunit SecA [1] (data from MRSA252) SACOL0303 5'-nucleotidase [1] (data from MRSA252) SACOL0552 hypothetical protein [1] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [1] (data from MRSA252) SACOL0742 hypothetical protein [1] (data from MRSA252) SACOL0944 NADH dehydrogenase [1] (data from MRSA252) SACOL1294 metallo-beta-lactamase [1] (data from MRSA252) SACOL1753 universal stress protein [1] (data from MRSA252) SACOL1952 ferritins family protein [1] (data from MRSA252)
⊟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): 0.001772
- TAT(Tat/SPI): 0.000201
- LIPO(Sec/SPII): 0.000209
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MPRKGSVPKRDVLPDPIHNSKLVTKLINKIMLDGKRGTAQRILYSAFDLVEQRSGRDALEVFEEAINNIMPVLEVKARRVGGSNYQVPVEVRPERRTTLGLRWLVNYARLRGEKTMEDRLANEILDAANNTGGAVKKREDTHKMAEANKAFAHYRW
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlasquantitative data / protein copy number per cell: 6838 [6]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟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: 7.22 h [7]
⊟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]
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 1.43 1.44
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) - ↑
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) - ↑
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)
⊟Relevant publications[edit | edit source]