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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00645
- pan locus tag?: SAUPAN002518000
- symbol: SAOUHSC_00645
- pan gene symbol?: tagD
- synonym:
- product: glycerol-3-phosphate cytidylyltransferase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3919937 NCBI
- RefSeq: YP_499205 NCBI
- BioCyc: G1I0R-601 BioCyc
- MicrobesOnline: 1289115 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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361ATGAAACGTGTAATAACATATGGCACATATGACTTACTTCACTATGGTCATATCGAATTG
CTTCGTCGTGCAAGAGAGATGGGCGATTATTTAATAGTAGCATTATCAACAGATGAATTT
AATCAAATTAAACATAAAAAATCTTATTATGATTATGAACAACGAAAAATGATGCTTGAA
TCAATACGCTATGTCGATTTAGTCATTCCAGAAAAGGGCTGGGGACAAAAAGAAGACGAT
GTCGAAAAATTTGATGTAGATGTTTTTGTTATGGGACATGACTGGGAAGGTGAATTCGAC
TTCTTAAAGGATAAATGTGAAGTCATTTATTTAAAACGTACAGAAGGCATTTCGACGACT
AAAATCAAACAAGAATTATATGGTAAAGATGCTAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00645
- symbol: SAOUHSC_00645
- description: glycerol-3-phosphate cytidylyltransferase
- length: 132
- theoretical pI: 5.69067
- theoretical MW: 15817
- GRAVY: -0.660606
⊟Function[edit | edit source]
- reaction: EC 2.7.7.39? ExPASyGlycerol-3-phosphate cytidylyltransferase CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol
- TIGRFAM: Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan glycerol-3-phosphate cytidylyltransferase (TIGR01518; EC 2.7.7.39; HMM-score: 201)and 5 morecytidyltransferase-like domain (TIGR00125; HMM-score: 77.8)Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides bifunctional protein RfaE, domain II (TIGR02199; EC 2.7.7.-; HMM-score: 61.5)Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A pantetheine-phosphate adenylyltransferase (TIGR01510; EC 2.7.7.3; HMM-score: 29.9)Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides nicotinate (nicotinamide) nucleotide adenylyltransferase (TIGR00482; EC 2.7.7.18; HMM-score: 15.2)nicotinamide-nucleotide adenylyltransferase (TIGR01526; EC 2.7.7.1; HMM-score: 13.8)
- TheSEED :
- Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39)
- PFAM: HUP (CL0039) CTP_transf_like; Cytidylyltransferase-like (PF01467; HMM-score: 83.6)and 3 moreFAD_syn; FAD synthetase (PF06574; HMM-score: 18.2)HIGH_NTase1_ass; Cytidyltransferase-related C-terminal region (PF16581; HMM-score: 14.9)Pantoate_ligase; Pantoate-beta-alanine ligase (PF02569; HMM-score: 13.8)
⊟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: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.003818
- TAT(Tat/SPI): 0.00017
- LIPO(Sec/SPII): 0.000723
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEKFDVDVFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTKIKQELYGKDAK
⊟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_00943 (ppnK) inorganic polyphosphate/ATP-NAD kinase [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [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)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- predicted SigA promoter [5] : SAOUHSC_00643 > SAOUHSC_00644 > SAOUHSC_00645
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] 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]
- ↑ 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) - ↑ 4.0 4.1 4.2 4.3 4.4 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 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)