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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00527
- pan locus tag?: SAUPAN002317000
- symbol: rpsL
- pan gene symbol?: rpsL
- synonym:
- product: 30S ribosomal protein S12
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920380 NCBI
- RefSeq: YP_499099 NCBI
- BioCyc: G1I0R-497 BioCyc
- MicrobesOnline: 1289009 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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361ATGCCAACTATTAACCAATTAGTACGTAAACCAAGACAAAGCAAAATCAAAAAATCAGAT
TCTCCAGCTTTAAATAAAGGTTTCAACAGTAAAAAGAAAAAATTTACTGACTTAAACTCA
CCACAAAAACGTGGTGTATGTACTCGTGTAGGTACAATGACACCTAAAAAACCTAACTCA
GCGTTACGTAAATATGCACGTGTGCGTTTATCAAACAACATCGAAATTAACGCATACATC
CCTGGTATCGGACATAACTTACAAGAACACAGTGTTGTACTTGTACGTGGTGGACGTGTA
AAAGACTTACCAGGTGTGCGTTACCATATTGTACGTGGAGCACTTGATACTTCAGGTGTT
GACGGACGTAGACAAGGTCGTTCATTATACGGAACTAAGAAACCTAAAAACTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00527
- symbol: RpsL
- description: 30S ribosomal protein S12
- length: 137
- theoretical pI: 11.8375
- theoretical MW: 15286.7
- GRAVY: -0.854015
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS12 (TIGR00981; HMM-score: 221.2)and 2 moreProtein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS12 (TIGR00982; HMM-score: 39.4)Protein synthesis Translation factors translation initiation factor IF-1 (TIGR00008; HMM-score: 13.4)
- TheSEED :
- SSU ribosomal protein S12p (S23e)
and 2 more - PFAM: OB (CL0021) Ribosom_S12_S23; Ribosomal protein S12/S23 (PF00164; HMM-score: 123.4)
⊟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): 0.029192
- TAT(Tat/SPI): 0.011807
- LIPO(Sec/SPII): 0.005124
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MPTINQLVRKPRQSKIKKSDSPALNKGFNSKKKKFTDLNSPQKRGVCTRVGTMTPKKPNSALRKYARVRLSNNIEINAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIVRGALDTSGVDGRRQGRSLYGTKKPKN
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [2] [3]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01201 (acpP) acyl carrier protein [4] (data from MRSA252) SAOUHSC_00790 (clpP) ATP-dependent Clp protease proteolytic subunit [4] (data from MRSA252) SAOUHSC_02380 (deoD) purine nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_02254 (groEL) chaperonin GroEL [4] (data from MRSA252) SAOUHSC_01159 (ileS) isoleucyl-tRNA synthetase [4] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [4] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [4] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [4] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [4] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00017 (rplI) 50S ribosomal protein L9 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [4] (data from MRSA252) SAOUHSC_02502 (rplN) 50S ribosomal protein L14 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_02505 (rplP) 50S ribosomal protein L16 [4] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [4] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [4] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [4] (data from MRSA252) SAOUHSC_01755 (rpmA) 50S ribosomal protein L27 [4] (data from MRSA252) SAOUHSC_01191 (rpmB) 50S ribosomal protein L28 [4] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [4] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_02487 (rpsM) 30S ribosomal protein S13 [4] (data from MRSA252) SAOUHSC_01250 (rpsO) 30S ribosomal protein S15 [4] (data from MRSA252) SAOUHSC_01208 (rpsP) 30S ribosomal protein S16 [4] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [4] (data from MRSA252) SAOUHSC_00350 (rpsR) 30S ribosomal protein S18 [4] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [4] (data from MRSA252) SAOUHSC_01689 (rpsT) 30S ribosomal protein S20 [4] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [4] (data from MRSA252) SAOUHSC_01216 (sucC) succinyl-CoA synthetase subunit beta [4] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [4] (data from MRSA252) SAOUHSC_01822 (tpx) 2-Cys peroxiredoxin [4] (data from MRSA252) SAOUHSC_00069 protein A [4] (data from MRSA252) SAOUHSC_00284 5'-nucleotidase [4] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [4] (data from MRSA252) SAOUHSC_00483 hypothetical protein [4] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00690 hypothetical protein [4] (data from MRSA252) SAOUHSC_00937 oligoendopeptidase F [4] (data from MRSA252) SAOUHSC_00951 hypothetical protein [4] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [4] (data from MRSA252) SAOUHSC_01035 hypothetical protein [4] (data from MRSA252) SAOUHSC_01228 transcriptional repressor CodY [4] (data from MRSA252) SAOUHSC_01252 hypothetical protein [4] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [4] (data from MRSA252) SAOUHSC_01327 catalase [4] (data from MRSA252) SAOUHSC_01587 ribosomal large subunit pseudouridine synthase B [4] (data from MRSA252) SAOUHSC_01632 glycine dehydrogenase subunit 2 [4] (data from MRSA252) SAOUHSC_01698 hypothetical protein [4] (data from MRSA252) SAOUHSC_01719 hypothetical protein [4] (data from MRSA252) SAOUHSC_01742 GTP pyrophosphokinase [4] (data from MRSA252) SAOUHSC_01814 hypothetical protein [4] (data from MRSA252) SAOUHSC_01820 acetate kinase [4] (data from MRSA252) SAOUHSC_02140 manganese-dependent inorganic pyrophosphatase [4] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_02381 hypothetical protein [4] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [4] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252) SAOUHSC_02504 50S ribosomal protein L29 [4] (data from MRSA252) SAOUHSC_02512a 30S ribosomal protein S10 [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252) SAOUHSC_02969 arginine deiminase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: rpoB > SAOUHSC_00525 > SAOUHSC_00526 > rpsL > SAOUHSC_00528 > SAOUHSC_00529 > SAOUHSC_00530predicted SigA promoter [5] : S183 > rplJ > rplL > S184 > SAOUHSC_00523 > S185 > rpoB > S186 > SAOUHSC_00525 > SAOUHSC_00526 > S187 > rpsL > SAOUHSC_00528 > S188 > SAOUHSC_00529 > S189 > SAOUHSC_00530predicted SigA promoter [5] : SAOUHSC_00523 > S185 > rpoB > S186 > SAOUHSC_00525 > SAOUHSC_00526 > S187 > rpsL > SAOUHSC_00528 > S188 > SAOUHSC_00529 > S189 > SAOUHSC_00530predicted SigA promoter [5] : S185 > rpoB > S186 > SAOUHSC_00525 > SAOUHSC_00526 > S187 > rpsL > SAOUHSC_00528 > S188 > SAOUHSC_00529 > S189 > SAOUHSC_00530predicted SigA promoter [5] : SAOUHSC_00526 > S187 > rpsL > SAOUHSC_00528 > S188 > SAOUHSC_00529 > S189 > SAOUHSC_00530
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] 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]
- ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
BMC Genomics: 2009, 10;291
[PubMed:19570206] [WorldCat.org] [DOI] (I e) - ↑ 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) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 4.46 4.47 4.48 4.49 4.50 4.51 4.52 4.53 4.54 4.55 4.56 4.57 4.58 4.59 4.60 4.61 4.62 4.63 4.64 4.65 4.66 4.67 4.68 4.69 4.70 4.71 4.72 4.73 4.74 4.75 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) - ↑ 5.0 5.1 5.2 5.3 5.4 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)
⊟Relevant publications[edit | edit source]
A Wada, H Watanabe
Penicillin-binding protein 1 of Staphylococcus aureus is essential for growth.
J Bacteriol: 1998, 180(10);2759-65
[PubMed:9573165] [WorldCat.org] [DOI] (P p)