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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
- pan locus tag?: SAUPAN002312000
- symbol: SACOL0587
- pan gene symbol?: rsmC
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
- symbol: SACOL0587
- product: hypothetical protein
- replicon: chromosome
- strand: +
- coordinates: 606165..606773
- length: 609
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236233 NCBI
- RefSeq: YP_185473 NCBI
- BioCyc: see SACOL_RS03045
- MicrobesOnline: 912067 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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601ATGAGTCATTATTACGATGAAGATCCAAGTGTAATTAGCAATGAACAACGTATTCAATAT
CAATTAAACCATCATAAAATTGATTTAATAACTGATAACGGAGTGTTTTCGAAAGATAAA
GTAGATTATGGTTCAGATGTTCTTGTTCAAACTTTTTTAAAAGCGCATCCACCTGGTCCA
AGTAAGCGAATTGCCGATGTTGGTTGTGGTTACGGACCAATTGGTTTGATGATTGCTAAA
GTATCACCACATCATTCAATTACAATGCTAGATGTTAATCACAGAGCGCTAGCCTTAGTT
GAAAAAAACAAAAAATTAAATGGTATTGATAATGTGATCGTAAAGGAAAGTGATGCTTTG
TCTGCTGTGGAAGACAAAAGTTTTGATTTTATTTTAACCAATCCACCAATAAGAGCAGGG
AAAGAAACCGTGCATCGTATATTCGAGCAAGCATTACATAGATTAGACTCGAACGGTGAA
CTATTCGTTGTAATTCAGAAGAAGCAAGGTATGCCATCTGCAAAGAAAAGAATGAATGAA
CTTTTTGGAAATGTAGAAGTGGTAAATAAAGATAAAGGATATTACATTCTGAGAAGTATA
AAAGCTTGA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
- symbol: SACOL0587
- description: hypothetical protein
- length: 202
- theoretical pI: 8.90035
- theoretical MW: 22679.8
- GRAVY: -0.378713
⊟Function[edit | edit source]
- TIGRFAM: Protein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 71.5)Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 59.8)and 24 moreProtein synthesis Ribosomal proteins: synthesis and modification protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific (TIGR03533; EC 2.1.1.-; HMM-score: 53.3)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: 38.7)Unknown function Enzymes of unknown specificity putative methylase (TIGR00537; HMM-score: 29.4)Biosynthesis of cofactors, prosthetic groups, and carriers Biotin malonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 28.9)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 3-demethylubiquinone-9 3-O-methyltransferase (TIGR01983; EC 2.1.1.64; HMM-score: 26.8)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone ubiquinone/menaquinone biosynthesis methyltransferase (TIGR01934; EC 2.1.1.-; HMM-score: 26.6)Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 22.7)Protein synthesis tRNA and rRNA base modification 23S rRNA (uracil-5-)-methyltransferase RumA (TIGR00479; EC 2.1.1.-; HMM-score: 22.3)Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG (TIGR00138; EC 2.1.1.170; HMM-score: 21.9)Protein synthesis tRNA and rRNA base modification 23S rRNA (uracil-5-)-methyltransferase RumB (TIGR02085; EC 2.1.1.189; HMM-score: 21.5)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone demethylmenaquinone methyltransferase (TIGR02752; EC 2.1.1.163; HMM-score: 21.2)Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides putative sugar O-methyltransferase (TIGR04371; EC 2.1.1.-; HMM-score: 18.9)Protein synthesis tRNA and rRNA base modification ribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 17.6)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll magnesium protoporphyrin O-methyltransferase (TIGR02021; EC 2.1.1.11; HMM-score: 17.6)Protein fate Protein modification and repair protein-L-isoaspartate O-methyltransferase (TIGR00080; EC 2.1.1.77; HMM-score: 16.5)Amino acid biosynthesis Aspartate family methionine biosynthesis protein MetW (TIGR02081; HMM-score: 16.3)Protein synthesis tRNA and rRNA base modification tRNA (guanine-N(7)-)-methyltransferase (TIGR00091; EC 2.1.1.33; HMM-score: 15.7)Protein synthesis tRNA and rRNA base modification 16S rRNA (cytosine(967)-C(5))-methyltransferase (TIGR00563; EC 2.1.1.176; HMM-score: 13.4)Protein synthesis tRNA and rRNA base modification N2,N2-dimethylguanosine tRNA methyltransferase (TIGR00308; EC 2.1.1.-; HMM-score: 13.2)methyltransferase, FkbM family (TIGR01444; HMM-score: 13.2)Protein synthesis Ribosomal proteins: synthesis and modification putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific (TIGR03704; EC 2.1.1.-; HMM-score: 11.9)Transcription RNA processing 3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 11.8)Protein synthesis tRNA and rRNA base modification 3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 11.8)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll C-20 methyltransferase BchU (TIGR02716; EC 2.1.1.-; HMM-score: 11.6)
- TheSEED :
- 16S rRNA (guanine(1207)-N(2))-methyltransferase (EC 2.1.1.172)
- PFAM: NADP_Rossmann (CL0063) MTS; Methyltransferase small domain (PF05175; HMM-score: 179)and 19 moreMethyltransf_31; Methyltransferase domain (PF13847; HMM-score: 51.4)Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 37)GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 29)Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 27.5)Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 27)Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 26.5)PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 25.2)Met_10; Met-10+ like-protein (PF02475; HMM-score: 22.4)Methyltransf_4; Putative methyltransferase (PF02390; HMM-score: 21.7)TehB; Tellurite resistance protein TehB (PF03848; HMM-score: 20.2)Methyltransf_16; Lysine methyltransferase (PF10294; HMM-score: 20)UPF0020; Putative RNA methylase family UPF0020 (PF01170; HMM-score: 19.2)TRM; N2,N2-dimethylguanosine tRNA methyltransferase (PF02005; HMM-score: 19.2)PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 18.7)Ubie_methyltran; ubiE/COQ5 methyltransferase family (PF01209; HMM-score: 18.2)Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 18)no clan defined MTS_N; Methyltransferase small domain N-terminal (PF08468; HMM-score: 17.8)NADP_Rossmann (CL0063) Methyltr_RsmB-F; 16S rRNA methyltransferase RsmB/F (PF01189; HMM-score: 17.5)Methyltransf_2; O-methyltransferase (PF00891; HMM-score: 11.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟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): 0.009464
- TAT(Tat/SPI): 0.000641
- LIPO(Sec/SPII): 0.00128
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MSHYYDEDPSVISNEQRIQYQLNHHKIDLITDNGVFSKDKVDYGSDVLVQTFLKAHPPGPSKRIADVGCGYGPIGLMIAKVSPHHSITMLDVNHRALALVEKNKKLNGIDNVIVKESDALSAVEDKSFDFILTNPPIRAGKETVHRIFEQALHRLDSNGELFVVIQKKQGMPSAKKRMNELFGNVEVVNKDKGYYILRSIKA
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 180 [4]
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟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: 41.63 h [5]
⊟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) - ↑ 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)