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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00521
- pan locus tag?: SAUPAN002311000
- symbol: rplL
- pan gene symbol?: rplL
- synonym:
- product: 50S ribosomal protein L7/L12
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920375 NCBI
- RefSeq: YP_499094 NCBI
- BioCyc: G1I0R-492 BioCyc
- MicrobesOnline: 1289004 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
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361ATGGCTAATCATGAACAAATCATTGAAGCGATTAAAGAAATGTCAGTATTAGAATTAAAC
GACTTAGTAAAAGCAATTGAAGAAGAATTTGGTGTAACTGCAGCTGCTCCAGTAGCAGTA
GCAGGTGCAGCTGGTGGCGCTGACGCTGCAGCAGAAAAAACTGAATTTGACGTTGAGTTA
ACTTCAGCTGGTTCATCTAAAATCAAAGTTGTTAAAGCTGTTAAAGAAGCAACTGGTTTA
GGATTAAAAGATGCTAAAGAATTAGTAGACGGAGCTCCTAAAGTAATCAAAGAAGCTTTA
CCTAAAGAAGAAGCTGAAAAACTTAAAGAACAATTAGAAGAAGTTGGAGCTACTGTAGAA
TTAAAATAA60
120
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00521
- symbol: RplL
- description: 50S ribosomal protein L7/L12
- length: 122
- theoretical pI: 4.32374
- theoretical MW: 12711.5
- GRAVY: -0.0483607
⊟Function[edit | edit source]
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bL12 (TIGR00855; HMM-score: 158.6)
- TheSEED :
- LSU ribosomal protein L7p/L12p (P1/P2)
- PFAM: no clan defined Ribosomal_L12; Ribosomal protein L7/L12 C-terminal domain (PF00542; HMM-score: 103.3)and 6 moreRibosomal_L12_N; Ribosomal protein L7/L12 dimerisation domain (PF16320; HMM-score: 75.9)IHF-likeDNA-bdg (CL0548) Bac_DNA_binding; Bacterial DNA-binding protein (PF00216; HMM-score: 15.3)no clan defined DUF2267; Uncharacterized conserved protein (DUF2267) (PF10025; HMM-score: 14.2)PP2C_C; Protein serine/threonine phosphatase 2C, C-terminal domain (PF07830; HMM-score: 13.3)PTS_IIA; PTS system, Lactose/Cellobiose specific IIA subunit (PF02255; HMM-score: 12.5)HTH (CL0123) HTH_33; Winged helix-turn helix (PF13592; HMM-score: 11.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 0.67
- Signal peptide possibility: -0.5
- N-terminally Anchored Score: -2
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.057639
- TAT(Tat/SPI): 0.076736
- LIPO(Sec/SPII): 0.001562
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MANHEQIIEAIKEMSVLELNDLVKAIEEEFGVTAAAPVAVAGAAGGADAAAEKTEFDVELTSAGSSKIKVVKAVKEATGLGLKDAKELVDGAPKVIKEALPKEEAEKLKEQLEEVGATVELK
⊟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_01683 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [4] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [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_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [4] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_02495 (rplR) 50S ribosomal protein L18 [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_02493 (rpmD) 50S ribosomal protein L30 [4] (data from MRSA252) SAOUHSC_00524 (rpoB) DNA-directed RNA polymerase subunit beta [4] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [4] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [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_00527 (rpsL) 30S ribosomal protein S12 [4] (data from MRSA252) SAOUHSC_02487 (rpsM) 30S ribosomal protein S13 [4] (data from MRSA252) SAOUHSC_00769 (secA) preprotein translocase subunit SecA [4] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [4] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [4] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [4] (data from MRSA252) SAOUHSC_00069 protein A [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00284 5'-nucleotidase [4] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [4] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00488 hypothetical protein [4] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00694 hypothetical protein [4] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_00906 hypothetical protein [4] (data from MRSA252) SAOUHSC_01029 phosphoenolpyruvate-protein phosphotransferase [4] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [4] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [4] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [4] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01251 polynucleotide phosphorylase/polyadenylase [4] (data from MRSA252) SAOUHSC_01337 transketolase [4] (data from MRSA252) SAOUHSC_01403 cold shock protein [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [4] (data from MRSA252) SAOUHSC_01653 superoxide dismutase [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [4] (data from MRSA252) SAOUHSC_01814 hypothetical protein [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_01820 acetate kinase [4] (data from MRSA252) SAOUHSC_01901 putative translaldolase [4] (data from MRSA252) SAOUHSC_01908 hypothetical protein [4] (data from MRSA252) SAOUHSC_02108 ferritin [4] (data from MRSA252) SAOUHSC_02131 hypothetical protein [4] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_02425 hypothetical protein [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_02542 molybdopterin biosynthesis protein MoeA [4] (data from MRSA252) SAOUHSC_02760 glutamate synthase subunit alpha [4] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [4] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [4] (data from MRSA252) SAOUHSC_02926 fructose-1,6-bisphosphate aldolase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: secE > SAOUHSC_00517 > rplK > rplA > rplJ > rplL > SAOUHSC_00523predicted SigA promoter [5] : S174 > gltX > S175 > S176 > SAOUHSC_00510 > cysS > SAOUHSC_00512 > SAOUHSC_00513 > SAOUHSC_00514 > S177 > SAOUHSC_00515 > S178 > S179 > secE > SAOUHSC_00517 > S180 > rplK > S181 > rplA > S182 > S183 > rplJ > rplLpredicted SigA promoter [5] : S179 > secE > SAOUHSC_00517 > S180 > rplK > S181 > rplA > S182 > S183 > rplJ > rplL > S184 > SAOUHSC_00523 > S185 > rpoB > S186 > SAOUHSC_00525predicted 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_00530
⊟Regulation[edit | edit source]
- regulator: L10 leader (transcription termination) regulon
L10 leader (5' cis-acting region) important in Ribosome biogenesis; transcription unit transferred from N315 data RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] Multi-gene expression profiles
⊟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]
- ↑ 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 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 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]
M Aboshkiwa, G Rowland, G Coleman
Nucleotide sequence of the Staphylococcus aureus RNA polymerase rpoB gene and comparison of its predicted amino acid sequence with those of other bacteria.
Biochim Biophys Acta: 1995, 1262(1);73-8
[PubMed:7772603] [WorldCat.org] [DOI] (P p)