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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1669 [new locus tag: SACOL_RS08515 ]
- pan locus tag?: SAUPAN004210000
- symbol: SACOL1669
- pan gene symbol?: —
- synonym:
- product: O-methyltransferase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1669 [new locus tag: SACOL_RS08515 ]
- symbol: SACOL1669
- product: O-methyltransferase
- replicon: chromosome
- strand: -
- coordinates: 1697218..1697856
- length: 639
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237550 NCBI
- RefSeq: YP_186509 NCBI
- BioCyc: see SACOL_RS08515
- MicrobesOnline: 913118 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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601ATGGATGACCTAAATAAAAAATATTTAATAGATTTACATCAACATCAAAATAGTTCAATC
GAAGTTTTGCGTGAATTTGCCGAGGTAAATGAAGTGCCAATTGTAGATCGTTTAACATTA
GATTTAATTAAGCAATTAATTCGTATGAATAATGTTAAAAATATTTTAGAAATTGGTACA
GCAATCGGCTATAGTTCTATGCAATTCGCTTCTATATCTGATGACATTCATGTCACAACG
ATAGAGCGTAATGAAACGATGATTCAATATGCTAAACAAAATTTAGCTACTTATCATTTT
GAAAACCAGGTTCGAATTATTGAAGGTAATGCTTTAGAGCAATTTGAAAATGTAAATGAC
AAAGTTTATGATATGATATTTATTGATGCAGCAAAAGCGCAATCAAAGAAATTTTTTGAA
ATATATACACCACTTTTAAAGCACCAAGGTCTCGTAATTACAGATAATGTTTTATATCAC
GGTTTTGTATCGGATATTGGGATTGTTAGATCGAGAAATGTAAGACAAATGGTTAAAAAG
GTTCAAGATTATAATGAGTGGTTAATAAAGCAACCAGGATATACAACGAATTTTTTAAAT
ATAGACGATGGATTAGCGATTTCAATTAAAGGAGAATGA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1669 [new locus tag: SACOL_RS08515 ]
- symbol: SACOL1669
- description: O-methyltransferase
- length: 212
- theoretical pI: 5.31765
- theoretical MW: 24526.8
- GRAVY: -0.255189
⊟Function[edit | edit source]
- TIGRFAM: 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: 40.9)Protein fate Protein modification and repair protein-L-isoaspartate O-methyltransferase (TIGR00080; EC 2.1.1.77; HMM-score: 33.3)and 13 moreProtein synthesis Ribosomal proteins: synthesis and modification protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific (TIGR03533; EC 2.1.1.-; HMM-score: 31.2)Protein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 27.3)Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG (TIGR00138; EC 2.1.1.170; HMM-score: 25.1)Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 24.9)methyltransferase, ATP-grasp peptide maturase system (TIGR04188; HMM-score: 23.1)Protein synthesis tRNA and rRNA base modification tRNA (guanine-N(7)-)-methyltransferase (TIGR00091; EC 2.1.1.33; HMM-score: 22.6)Protein synthesis tRNA and rRNA base modification ribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 21.7)Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD (TIGR00095; EC 2.1.1.171; HMM-score: 18)Biosynthesis of cofactors, prosthetic groups, and carriers Biotin malonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 17.7)methyltransferase, FxLD system (TIGR04364; HMM-score: 17.3)Unknown function Enzymes of unknown specificity tRNA (cmo5U34)-methyltransferase (TIGR00740; EC 2.1.1.-; HMM-score: 15.9)pseudaminic acid biosynthesis-associated methylase (TIGR03587; HMM-score: 15.5)methyltransferase, FkbM family (TIGR01444; HMM-score: 13.3)
- TheSEED :
- FIG011945: O-methyltransferase family protein
- PFAM: NADP_Rossmann (CL0063) Methyltransf_3; O-methyltransferase (PF01596; HMM-score: 91.9)and 17 moreMethyltransf_24; Methyltransferase domain (PF13578; HMM-score: 47.3)Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 46.9)PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 35.9)Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 28.9)MTS; Methyltransferase small domain (PF05175; HMM-score: 27.6)GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 26.4)Cons_hypoth95; Conserved hypothetical protein 95 (PF03602; HMM-score: 26.2)Methyltransf_4; Putative methyltransferase (PF02390; HMM-score: 25.9)Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 24)Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 23.2)Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 22.8)CMAS; Mycolic acid cyclopropane synthetase (PF02353; HMM-score: 21.7)Methyltransf_15; RNA cap guanine-N2 methyltransferase (PF09445; HMM-score: 20.9)Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase (PF00070; HMM-score: 17.5)Met_10; Met-10+ like-protein (PF02475; HMM-score: 16.8)RrnaAD; Ribosomal RNA adenine dimethylase (PF00398; HMM-score: 16.5)Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 12.9)
⊟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): 0.004664
- TAT(Tat/SPI): 0.000192
- LIPO(Sec/SPII): 0.000152
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MDDLNKKYLIDLHQHQNSSIEVLREFAEVNEVPIVDRLTLDLIKQLIRMNNVKNILEIGTAIGYSSMQFASISDDIHVTTIERNETMIQYAKQNLATYHFENQVRIIEGNALEQFENVNDKVYDMIFIDAAKAQSKKFFEIYTPLLKHQGLVITDNVLYHGFVSDIGIVRSRNVRQMVKKVQDYNEWLIKQPGYTTNFLNIDDGLAISIKGE
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 37 [4]
- interaction partners:
⊟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]
⊟Protein stability[edit | edit source]
- half-life: 13.88 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)