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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00475
- pan locus tag?: SAUPAN002243000
- symbol: SAOUHSC_00475
- pan gene symbol?: pth
- synonym:
- product: peptidyl-tRNA hydrolase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920335 NCBI
- RefSeq: YP_499054 NCBI
- BioCyc: G1I0R-441 BioCyc
- MicrobesOnline: 1288952 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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541ATGAAATGTATTGTAGGTCTAGGTAATATAGGTAAACGTTTTGAACTTACAAGACATAAT
ATCGGCTTTGAAGTCGTTGATTATATTTTAGAGAAAAATAATTTTTCATTAGATAAACAA
AAGTTTAAAGGTGCATATACAATTGAACGAATGAACGGCGATAAAGTGTTATTTATCGAA
CCAATGACAATGATGAATTTGTCAGGTGAAGCAGTTGCACCGATTATGGATTATTACAAT
GTTAATCCAGAAGATTTAATTGTCTTATATGATGATTTAGATTTAGAACAAGGACAAGTT
CGCTTAAGACAAAAAGGAAGTGCGGGCGGTCACAATGGTATGAAATCAATTATTAAAATG
CTTGGTACAGACCAATTTAAACGTATTCGTATTGGTGTGGGAAGACCAACGAATGGTATG
ACGGTACCTGATTATGTTTTACAACGCTTTTCAAATGATGAAATGGTAACGATGGAAAAA
GTTATCGAACACGCAGCACGCGCAATTGAAAAGTTTGTTGAAACATCACGATTTGACCAT
GTTATGAATGAATTTAATGGTGAAGTGAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00475
- symbol: SAOUHSC_00475
- description: peptidyl-tRNA hydrolase
- length: 190
- theoretical pI: 6.52772
- theoretical MW: 21702.9
- GRAVY: -0.344211
⊟Function[edit | edit source]
- reaction: EC 3.1.1.29? ExPASyAminoacyl-tRNA hydrolase N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
- TIGRFAM: Protein synthesis Other aminoacyl-tRNA hydrolase (TIGR00447; EC 3.1.1.29; HMM-score: 214.1)
- TheSEED :
- Peptidyl-tRNA hydrolase (EC 3.1.1.29)
Dormancy and Sporulation Dormancy and Sporulation - no subcategory Sporulation-associated proteins with broader functions Peptidyl-tRNA hydrolase (EC 3.1.1.29)and 1 more - PFAM: no clan defined Pept_tRNA_hydro; Peptidyl-tRNA hydrolase (PF01195; HMM-score: 192.3)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 10
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0
- Extracellular Score: 0
- 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): 0.003218
- TAT(Tat/SPI): 0.000092
- LIPO(Sec/SPII): 0.000418
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKCIVGLGNIGKRFELTRHNIGFEVVDYILEKNNFSLDKQKFKGAYTIERMNGDKVLFIEPMTMMNLSGEAVAPIMDYYNVNPEDLIVLYDDLDLEQGQVRLRQKGSAGGHNGMKSIIKMLGTDQFKRIRIGVGRPTNGMTVPDYVLQRFSNDEMVTMEKVIEHAARAIEKFVETSRFDHVMNEFNGEVK
⊟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_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_02116 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [4] (data from MRSA252) SAOUHSC_02254 (groEL) chaperonin GroEL [4] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [4] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [4] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [4] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [4] (data from MRSA252) SAOUHSC_01785 (rpmI) 50S ribosomal protein L35 [4] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [4] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [4] (data from MRSA252) SAOUHSC_02498 (rpsH) 30S ribosomal protein S8 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_00350 (rpsR) 30S ribosomal protein S18 [4] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [4] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [4] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [4] (data from MRSA252) SAOUHSC_02353 (upp) uracil phosphoribosyltransferase [4] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [4] (data from MRSA252) SAOUHSC_00195 acetyl-CoA acetyltransferase [4] (data from MRSA252) SAOUHSC_00196 hypothetical protein [4] (data from MRSA252) SAOUHSC_00284 5'-nucleotidase [4] (data from MRSA252) SAOUHSC_00346 GTP-dependent nucleic acid-binding protein EngD [4] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [4] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [4] (data from MRSA252) SAOUHSC_00488 hypothetical protein [4] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [4] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [4] (data from MRSA252) SAOUHSC_00529 elongation factor G [4] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [4] (data from MRSA252) SAOUHSC_00634 ABC transporter substrate-binding protein [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00845 hypothetical protein [4] (data from MRSA252) SAOUHSC_00878 hypothetical protein [4] (data from MRSA252) SAOUHSC_01035 hypothetical protein [4] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [4] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [4] (data from MRSA252) SAOUHSC_01071 glycerophosphoryl diester phosphodiesterase [4] (data from MRSA252) SAOUHSC_01100 thioredoxin [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [4] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [4] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [4] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_01814 hypothetical protein [4] (data from MRSA252) SAOUHSC_01819 hypothetical protein [4] (data from MRSA252) SAOUHSC_01845 formate--tetrahydrofolate ligase [4] (data from MRSA252) SAOUHSC_01909 S-adenosylmethionine synthetase [4] (data from MRSA252) SAOUHSC_02176 hypothetical protein [4] (data from MRSA252) SAOUHSC_02363 aldehyde dehydrogenase [4] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [4] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [4] (data from MRSA252) SAOUHSC_02512a 30S ribosomal protein S10 [4] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [4] (data from MRSA252) SAOUHSC_02860 HMG-CoA synthase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_00474 > SAOUHSC_00475 > SAOUHSC_00477 > SAOUHSC_00479 > SAOUHSC_00480 > SAOUHSC_00481 > SAOUHSC_00482 > SAOUHSC_00483predicted SigA promoter [5] : S158 > SAOUHSC_00475 > SAOUHSC_00477 > SAOUHSC_00479 > SAOUHSC_00480 > SAOUHSC_00481 > SAOUHSC_00482 > SAOUHSC_00483 > S159 > SAOUHSC_00484
⊟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) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 4.46 4.47 4.48 4.49 4.50 4.51 4.52 4.53 4.54 4.55 4.56 4.57 4.58 4.59 4.60 4.61 4.62 4.63 4.64 4.65 4.66 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)