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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1683 [new locus tag: SACOL_RS08585 ]
- pan locus tag?: SAUPAN004231000
- symbol: SACOL1683
- pan gene symbol?: tcdA
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1683 [new locus tag: SACOL_RS08585 ]
- symbol: SACOL1683
- product: hypothetical protein
- replicon: chromosome
- strand: -
- coordinates: 1712034..1712807
- length: 774
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238611 NCBI
- RefSeq: YP_186523 NCBI
- BioCyc: see SACOL_RS08585
- MicrobesOnline: 913132 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
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 721ATGAAACATCAATTTTCAAGAAATGAACTAGCGATTGGACAACAAGGTTTAGATTTATTG
 AAGCAACAAACTGTTGTCATACTTGGCGTTGGAGGTGTTGGTTCATTTGCTGCTGAAGCA
 TTAGCAAGAACGAATATTGGTCATATTATATTAATAGATAAAGATGATGTTGATATTACA
 AATGTAAACAGACAATTACACGCTTTAACTACAACGGTAGGACAAAGTAAAGTTTCTTTG
 ATGGAAGAACGTATTAAATTAATTAATCCAGATTGTAAAGTCACGCCCTTACATATGTTT
 TATACAGAAGAGACATATGAAGAAATTTTCGATAACTACGATATAGATTATTTTGTAGAT
 GCAAGTGATACAATAATGTACAAAGTACACTTAATGAAAGAGTGTCTTGACCGAGGGATT
 AAAGTGATTTCCAGTATGGGTGCTGCAAATAAAACAGATCCAACACGTTTTACAATTTCA
 GATATCTCTAAAACACATACCGATCCAATGGCCAAAATTATTCGTCAAAAATTGAAAAAA
 CTAGGAATTCGTAAAGGGATTCCAGTTGTATTTTCAGATGAAAGTCCAATTGTCATAAGA
 GAAGATGTAAAAGATATAGTTGGAGATAAAAATGCTATCAATCGAAAAGGACAAATGCCA
 CCTTCTTCAAATGCCTTTGTGCCAAGTGTTGTTGGATTAATTTGTGCAAGTTATGTGGTG
 AATGACGTATTAAAAGATATTCCAGTTCGTCGCATTAAAGACAAAGGGCAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1683 [new locus tag: SACOL_RS08585 ]
- symbol: SACOL1683
- description: hypothetical protein
- length: 257
- theoretical pI: 8.07957
- theoretical MW: 28641
- GRAVY: -0.161479
⊟Function[edit | edit source]
- TIGRFAM: Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiazole biosynthesis adenylyltransferase ThiF (TIGR02356; EC 2.7.7.73; HMM-score: 84.2)Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdopterin synthase sulfurylase MoeB (TIGR02355; HMM-score: 77.6)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiamine biosynthesis protein ThiF (TIGR02354; HMM-score: 72.9)and 10 morePRTRC system ThiF family protein (TIGR03736; HMM-score: 24.1)ubiquitin-activating enzyme E1 (TIGR01408; HMM-score: 19.5)E1-like protein-activating enzyme Gsa7p/Apg7p (TIGR01381; HMM-score: 18.3)Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin glutamyl-tRNA reductase (TIGR01035; EC 1.2.1.70; HMM-score: 17.2)Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A 2-dehydropantoate 2-reductase (TIGR00745; EC 1.1.1.-; HMM-score: 16.1)Cellular processes Detoxification S-(hydroxymethyl)mycothiol dehydrogenase (TIGR03451; EC 1.1.1.306; HMM-score: 15.3)Protein fate Protein folding and stabilization xanthine dehydrogenase accessory protein XdhC (TIGR02964; HMM-score: 14.3)Purines, pyrimidines, nucleosides, and nucleotides Other xanthine dehydrogenase accessory protein XdhC (TIGR02964; HMM-score: 14.3)6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase (TIGR03201; EC 1.1.1.-; HMM-score: 13.5)Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll geranylgeranyl reductase family (TIGR02032; EC 1.3.1.-; HMM-score: 12.1)
- TheSEED  : - tRNA threonylcarbamoyladenosine dehydratase
 
- PFAM: NADP_Rossmann (CL0063) ThiF; ThiF family (PF00899; HMM-score: 128.2)and 10 moreSacchrp_dh_NADP; Saccharopine dehydrogenase NADP binding domain (PF03435; HMM-score: 20.8)TrkA_N; TrkA-N domain (PF02254; HMM-score: 17.9)ApbA; Ketopantoate reductase PanE/ApbA (PF02558; HMM-score: 16.9)Shikimate_DH; Shikimate / quinate 5-dehydrogenase (PF01488; HMM-score: 14.1)2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 14)no clan defined UbiD_C; 3-octaprenyl-4-hydroxybenzoate carboxy-lyase C-terminal domain (PF20696; HMM-score: 13)NADP_Rossmann (CL0063) AlaDh_PNT_C; Alanine dehydrogenase/PNT, C-terminal domain (PF01262; HMM-score: 12.5)ELFV_dehydrog; Glutamate/Leucine/Phenylalanine/Valine dehydrogenase (PF00208; HMM-score: 12)DAO; FAD dependent oxidoreductase (PF01266; HMM-score: 11.8)Trp_halogenase; Tryptophan halogenase (PF04820; HMM-score: 10.5)
⊟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
 
- DeepLocPro: Cytoplasmic- Cytoplasmic Score: 0.9575
- Cytoplasmic Membrane Score: 0.0194
- Cell wall & surface Score: 0.0001
- Extracellular Score: 0.0231
 
- LocateP: Intracellular - Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: -2
- Predicted Cleavage Site: No CleavageSite
 
- SignalP: no predicted signal peptide- SP(Sec/SPI): 0.236347
- TAT(Tat/SPI): 0.292054
- LIPO(Sec/SPII): 0.002753
 
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKHQFSRNELAIGQQGLDLLKQQTVVILGVGGVGSFAAEALARTNIGHIILIDKDDVDITNVNRQLHALTTTVGQSKVSLMEERIKLINPDCKVTPLHMFYTEETYEEIFDNYDIDYFVDASDTIMYKVHLMKECLDRGIKVISSMGAANKTDPTRFTISDISKTHTDPMAKIIRQKLKKLGIRKGIPVVFSDESPIVIREDVKDIVGDKNAINRKGQMPPSSNAFVPSVVGLICASYVVNDVLKDIPVRRIKDKGQ
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 568 [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: 26.85 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 can add further information about the gene and protein here. [edit]
⊟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)