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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00346
- pan locus tag?: SAUPAN001909000
- symbol: SAOUHSC_00346
- pan gene symbol?: ychF
- synonym:
- product: GTP-dependent nucleic acid-binding protein EngD
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00346
- symbol: SAOUHSC_00346
- product: GTP-dependent nucleic acid-binding protein EngD
- replicon: chromosome
- strand: +
- coordinates: 359012..360109
- length: 1098
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921819 NCBI
- RefSeq: YP_498935 NCBI
- BioCyc: G1I0R-321 BioCyc
- MicrobesOnline: 1288829 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1081ATGGCTTTAACAGCAGGTATCGTTGGATTGCCAAACGTTGGTAAATCAACATTATTTAAT
GCAATAACAAAAGCAGGTGCTTTAGCAGCGAACTATCCATTCGCTACGATTGATCCTAAT
GTAGGGATAGTAGAAGTGCCAGATGCTAGATTACTTAAATTAGAAGAAATGGTTCAACCT
AAAAAGACATTGCCGACTACATTTGAATTTACAGATATCGCTGGTATTGTGAAAGGTGCT
TCAAAGGGAGAAGGGTTAGGTAATAAATTCTTATCACATATTAGAGAAGTAGATGCGATT
TGTCAGGTCGTTCGTGCATTTGATGATGATAACGTAACTCATGTTGCTGGTCGAGTAGAC
CCTATTGATGATATTGAAGTTATTAATATGGAATTAGTACTAGCGGACTTAGAATCTGTT
GAGAAACGTTTGCCTAGAATTGAAAAATTAGCACGTCAAAAAGATAAGACTGCTGAAATG
GAAGTACGTATTTTAACAACTATTAAAGAAGCTTTAGAAAATGGTAAACCCGCTCGTAGT
ATTGACTTTAATGAAGAAGATCAAAAATGGGTGAATCAAGCGCAATTACTGACTTCTAAA
AAAATGCTTTATATCGCTAATGTTGGTGAAGATGAAATTGGTGATGATGATAATGATAAA
GTAAAAGCGATTCGTGAATATGCAGCGCAAGAAGACTCTGAAGTGATTGTTATTAGTGCA
AAAATTGAAGAAGAAATTGCTACATTAGATGATGAAGATAAAGAAATGTTCTTAGAAGAT
TTAGGTATCGAAGAACCAGGATTAGATCGATTAATTAGAACAACTTATGAATTATTAGGA
TTATCAACATATTTTACTGCTGGTGTGCAAGAAGTACGTGCTTGGACATTTAAACAAGGT
ATGACTGCACCTCAATGTGCTGGTATCATTCATACTGATTTTGAACGTGGATTTATCCGT
GCCGAAGTAACAAGTTATGACGACTATGTACAATATGGTGGCGAAAGTGGCGCTAAAGAA
GCGGGCAGACAACGATTAGAAGGTAAAGAATATATTATGCAAGATGGCGATATCGTTCAT
TTCAGATTTAATGTATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00346
- symbol: SAOUHSC_00346
- description: GTP-dependent nucleic acid-binding protein EngD
- length: 365
- theoretical pI: 4.33991
- theoretical MW: 40594.7
- GRAVY: -0.288767
⊟Function[edit | edit source]
- TIGRFAM: Unknown function General GTP-binding protein YchF (TIGR00092; HMM-score: 516.4)and 11 moreProtein synthesis Other Obg family GTPase CgtA (TIGR02729; HMM-score: 80.9)Unknown function General GTP-binding protein HflX (TIGR03156; HMM-score: 37.8)Unknown function General small GTP-binding protein domain (TIGR00231; HMM-score: 33.3)Protein synthesis Other ribosome-associated GTPase EngA (TIGR03594; HMM-score: 30.9)Transport and binding proteins Cations and iron carrying compounds ferrous iron transport protein B (TIGR00437; HMM-score: 27.9)Protein synthesis Other ribosome biogenesis GTP-binding protein YlqF (TIGR03596; HMM-score: 24.4)Protein synthesis Other GTP-binding protein Era (TIGR00436; HMM-score: 20.9)Protein fate Protein modification and repair [FeFe] hydrogenase H-cluster maturation GTPase HydF (TIGR03918; HMM-score: 19.2)Protein synthesis tRNA and rRNA base modification tRNA modification GTPase TrmE (TIGR00450; EC 3.6.-.-; HMM-score: 14.1)Protein synthesis Other ribosome biogenesis GTP-binding protein YsxC (TIGR03598; HMM-score: 14.1)Protein synthesis Other ribosome biogenesis GTPase YqeH (TIGR03597; HMM-score: 13.5)
- TheSEED :
- GTP-binding and nucleic acid-binding protein YchF
- PFAM: Ubiquitin (CL0072) YchF-GTPase_C; Protein of unknown function (DUF933) (PF06071; HMM-score: 136.6)and 3 moreP-loop_NTPase (CL0023) MMR_HSR1; 50S ribosome-binding GTPase (PF01926; HMM-score: 83.5)FeoB_N; Ferrous iron transport protein B (PF02421; HMM-score: 33.1)Ubiquitin (CL0072) TGS; TGS domain (PF02824; HMM-score: 15.5)
⊟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: 0.67
- Signal peptide possibility: -0.5
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.140842
- TAT(Tat/SPI): 0.037919
- LIPO(Sec/SPII): 0.009151
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MALTAGIVGLPNVGKSTLFNAITKAGALAANYPFATIDPNVGIVEVPDARLLKLEEMVQPKKTLPTTFEFTDIAGIVKGASKGEGLGNKFLSHIREVDAICQVVRAFDDDNVTHVAGRVDPIDDIEVINMELVLADLESVEKRLPRIEKLARQKDKTAEMEVRILTTIKEALENGKPARSIDFNEEDQKWVNQAQLLTSKKMLYIANVGEDEIGDDDNDKVKAIREYAAQEDSEVIVISAKIEEEIATLDDEDKEMFLEDLGIEEPGLDRLIRTTYELLGLSTYFTAGVQEVRAWTFKQGMTAPQCAGIIHTDFERGFIRAEVTSYDDYVQYGGESGAKEAGRQRLEGKEYIMQDGDIVHFRFNV
⊟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:
SAOUHSC_02318 (ddl) D-alanyl-alanine synthetase A [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00574 (eutD) phosphotransacetylase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_02116 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [3] (data from MRSA252) SAOUHSC_00225 (ispD) 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [3] (data from MRSA252) SAOUHSC_00493 (lysS) lysyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01755 (rpmA) 50S ribosomal protein L27 [3] (data from MRSA252) SAOUHSC_02493 (rpmD) 50S ribosomal protein L30 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02498 (rpsH) 30S ribosomal protein S8 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_02487 (rpsM) 30S ribosomal protein S13 [3] (data from MRSA252) SAOUHSC_01250 (rpsO) 30S ribosomal protein S15 [3] (data from MRSA252) SAOUHSC_00350 (rpsR) 30S ribosomal protein S18 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01216 (sucC) succinyl-CoA synthetase subunit beta [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [3] (data from MRSA252) SAOUHSC_02353 (upp) uracil phosphoribosyltransferase [3] (data from MRSA252) SAOUHSC_00002 DNA polymerase III subunit beta [3] (data from MRSA252) SAOUHSC_00009 seryl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00284 5'-nucleotidase [3] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [3] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00472 ribose-phosphate pyrophosphokinase [3] (data from MRSA252) SAOUHSC_00485 hypoxanthine phosphoribosyltransferase [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00562 phosphomethylpyrimidine kinase [3] (data from MRSA252) SAOUHSC_00634 ABC transporter substrate-binding protein [3] (data from MRSA252) SAOUHSC_00690 hypothetical protein [3] (data from MRSA252) SAOUHSC_00767 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00798 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [3] (data from MRSA252) SAOUHSC_00835 hypothetical protein [3] (data from MRSA252) SAOUHSC_00847 ABC transporter ATP-binding protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [3] (data from MRSA252) SAOUHSC_01029 phosphoenolpyruvate-protein phosphotransferase [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01199 3-oxoacyl-(acyl-carrier-protein) reductase [3] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [3] (data from MRSA252) SAOUHSC_01337 transketolase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01451 threonine dehydratase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02337 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02512a 30S ribosomal protein S10 [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [3] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [3] (data from MRSA252) SAOUHSC_02926 fructose-1,6-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟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) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 3.62 3.63 3.64 3.65 3.66 3.67 3.68 3.69 3.70 3.71 3.72 3.73 3.74 3.75 3.76 3.77 3.78 3.79 3.80 3.81 3.82 3.83 3.84 3.85 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) - ↑ 4.0 4.1 4.2 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)