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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01681
- pan locus tag?: SAUPAN004161000
- symbol: prmA
- pan gene symbol?: prmA
- synonym:
- product: ribosomal protein L11 methyltransferase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01681
- symbol: prmA
- product: ribosomal protein L11 methyltransferase
- replicon: chromosome
- strand: -
- coordinates: 1590396..1591334
- length: 939
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921793 NCBI
- RefSeq: YP_500191 NCBI
- BioCyc: G1I0R-1562 BioCyc
- MicrobesOnline: 1290105 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGAACTGGACAGAGCTTTCAATTATTATTAATCATGAAGCAGTAGAATTGGCTACCAAT
ATACTTGAAAATCATGGATCAAATGGTGTCGTGATAGAAGATTCAGATGATTTAATTAAC
CAACCAGAAGATAAATACGGTGAAATTTACGCTTTGAAAAAAGAGGATTATCCAGATAAG
GGAGTAAGATTGAAAGCCTATTTTAATGAAATGACTTATGATGATAAGTTGCGACAGCAA
ATTAAAGATGAGTTATTAAATTTAGATGAACTTGATCAACATAACGTTCAATTCAGTGAG
CAAATTATTGCAGAGACGGATTGGGAAAATGAATGGAAAAACTATTTCCATCCATTCCGA
GCGTCGAAGAAGTTCACAATAGTTCCTAGTTGGGAAACATATGCTAAAGAAGCGGATGAA
GAGCTTTGCATTGAGCTCGACCCAGGTATGGCTTTTGGAACAGGTGATCATCCGACTACA
AGTATGTGTTTGAAGGCAATAGAAACATATGTATTGCCACAGCATTCAGTAATTGATGTT
GGTACTGGCTCAGGTATATTAAGTATTGCAAGTCATCTAATCGGTGTAAAACGTATTAAA
GCGTTGGATATTGATGAAATGGCAGTGAGTGTAGCTAAAGAAAACTTCAGAAGAAATCAT
TGTGAAACGTTAATTGAAGCTGTTCCAGGTAACTTATTGAAAGACGAAACAGAAAAATTT
GATATTGTAATAGCAAATATTTTAGCGCATATTATTGATGAAATGATTGAAGATGCTTAT
AATACTCTAAATGAAGGCGGTTATTTTATTACTTCTGGTATTATAAAAGAGAAGTATGAA
GGTATACAGTCACATATGGAGCGTGTAGGTTTTAAAATTATTTCAGAACAACATGACAAC
GGTTGGGTTTGTCTTGTTGGCCAGAAAGTGAGTGAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01681
- symbol: PrmA
- description: ribosomal protein L11 methyltransferase
- length: 312
- theoretical pI: 4.33956
- theoretical MW: 35512.7
- GRAVY: -0.376923
⊟Function[edit | edit source]
- reaction: EC 2.1.1.-? ExPASy
- TIGRFAM: Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 257.9)and 13 moreProtein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 45.4)Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 39.6)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 3-demethylubiquinone-9 3-O-methyltransferase (TIGR01983; EC 2.1.1.64; HMM-score: 37.6)Protein synthesis Ribosomal proteins: synthesis and modification protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific (TIGR03533; EC 2.1.1.-; HMM-score: 37.6)Unknown function Enzymes of unknown specificity putative methylase (TIGR00537; HMM-score: 36.7)Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit (TIGR02469; EC 2.1.1.132; HMM-score: 32)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll magnesium protoporphyrin O-methyltransferase (TIGR02021; EC 2.1.1.11; HMM-score: 30.5)Biosynthesis of cofactors, prosthetic groups, and carriers Biotin malonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 24.5)methyltransferase, ATP-grasp peptide maturase system (TIGR04188; HMM-score: 18.3)Protein synthesis Ribosomal proteins: synthesis and modification putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific (TIGR03704; EC 2.1.1.-; HMM-score: 17)Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG (TIGR00138; EC 2.1.1.170; HMM-score: 16.2)Protein synthesis tRNA and rRNA base modification ribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 15.5)Hypothetical proteins Conserved putative methyltransferase, TIGR01177 family (TIGR01177; HMM-score: 14.6)
- TheSEED :
- Ribosomal protein L11 methyltransferase (EC 2.1.1.-)
Protein Metabolism Protein biosynthesis Ribosome biogenesis bacterial Ribosomal protein L11 methyltransferase (EC 2.1.1.-)and 1 more - PFAM: NADP_Rossmann (CL0063) PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 355.5)and 14 moreMTS; Methyltransferase small domain (PF05175; HMM-score: 55.4)Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 40.1)Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 36.3)Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 35.9)Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 30.9)Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 28)Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 24.8)Met_10; Met-10+ like-protein (PF02475; HMM-score: 18.6)Spermine_synth; Spermine/spermidine synthase domain (PF01564; HMM-score: 17.7)PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 17.4)Cons_hypoth95; Conserved hypothetical protein 95 (PF03602; HMM-score: 15.7)UPF0020; Putative RNA methylase family UPF0020 (PF01170; HMM-score: 13)GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 12.9)TRM; N2,N2-dimethylguanosine tRNA methyltransferase (PF02005; HMM-score: 12)
⊟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: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: -1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.007117
- TAT(Tat/SPI): 0.000217
- LIPO(Sec/SPII): 0.000972
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MNWTELSIIINHEAVELATNILENHGSNGVVIEDSDDLINQPEDKYGEIYALKKEDYPDKGVRLKAYFNEMTYDDKLRQQIKDELLNLDELDQHNVQFSEQIIAETDWENEWKNYFHPFRASKKFTIVPSWETYAKEADEELCIELDPGMAFGTGDHPTTSMCLKAIETYVLPQHSVIDVGTGSGILSIASHLIGVKRIKALDIDEMAVSVAKENFRRNHCETLIEAVPGNLLKDETEKFDIVIANILAHIIDEMIEDAYNTLNEGGYFITSGIIKEKYEGIQSHMERVGFKIISEQHDNGWVCLVGQKVSE
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- predicted SigA promoter [3] : rpsU < S664 < S665 < SAOUHSC_01679 < SAOUHSC_01680 < prmA < SAOUHSC_01682 < S666 < dnaK < SAOUHSC_01684 < SAOUHSC_01685
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [3] 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]
- ↑ 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) - ↑ 3.0 3.1 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) - ↑ Arnaud Chastanet, Juliette Fert, Tarek Msadek
Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria.
Mol Microbiol: 2003, 47(4);1061-73
[PubMed:12581359] [WorldCat.org] [DOI] (P p)