NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

organism: Staphylococcus aureus NCTC8325

locus tag: SAOUHSC_00100

pan locus tag^?: SAUPAN000950000

symbol: SAOUHSC_00100

pan gene symbol^?: deoC1

synonym:
product: 2-deoxyribose-5-phosphate aldolase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

type: CDS
locus tag: SAOUHSC_00100
symbol: SAOUHSC_00100
product: 2-deoxyribose-5-phosphate aldolase
replicon: chromosome
strand: +
coordinates: 104508..105170
length: 663
essential: no ^[1] DEG other strains

⊟Accession numbers[edit | edit source]

Gene ID: 3919809 NCBI
RefSeq: YP_498700 NCBI
BioCyc: G1I0R-92 BioCyc
MicrobesOnline: 1288594 MicrobesOnline

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

1
61
121
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241
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361
421
481
541
601
661
ATGAAATTTGAGAAATATATAGATCACACTTTATTGAAGCCTGAGTCAACACGTACGCAA
ATCGATCAAATCATCGATGAAGCGAAAGCATACAATTTTAAATCTGTATGTGTGAATCCA
ACACATGTTAAATATGCAGCAGAGCGACTAGCTGATTCAGAGGTGCTCGTTTGTACGGTA
ATAGGATTCCCATTAGGTGCGTCGACAACTGCAACGAAAGCATTTGAAACAGAAGATGCA
ATTCAAAATGGTGCAGATGAAATTGACATGGTCATCAACATCGGCGCATTAAAAGATGGA
CGTTTTGATGATGTACAACAAGACATTGAAGCAGTGGTTAAAGCTGCGAAAGGTCACACA
GTAAAAGTGATTATTGAGACGGTATTGTTGGACCATGACGAAATTGTAAAAGCGAGTGAA
TTAACAAAAGCGGCTGGTGCGGACTTCGTTAAAACTTCAACAGGTTTTGCAGGTGGCGGT
GCGACTGCAGAAGACGTTAAATTAATGAAAGATACAGTAGGTGCTGATGTAGAAGTAAAA
GCATCAGGTGGCGTACGTAATTTAGAAGATTTCAATAAAATGGTTGAAGCAGGTGCGACA
CGTATTGGTGCGAGCGCAGGTGTTCAAATTATGCAAGGTTTAGAAGCAGATTCAGATTAC
TAA
60
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240
300
360
420
480
540
600
660
663

⊟Protein[edit | edit source]

⊟General[edit | edit source]

locus tag: SAOUHSC_00100
symbol: SAOUHSC_00100
description: 2-deoxyribose-5-phosphate aldolase
length: 220
theoretical pI: 4.43408
theoretical MW: 23472.3
GRAVY: -0.109091

⊟Function[edit | edit source]

⊞reaction:
EC 4.1.2.4? ExPASy
Deoxyribose-phosphate aldolase 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
⊞TIGRFAM:
Metabolism Energy metabolism Other deoxyribose-phosphate aldolase (TIGR00126; EC 4.1.2.4; HMM-score: 288.5)
Metabolism Purines, pyrimidines, nucleosides, and nucleotides Other deoxyribose-phosphate aldolase (TIGR00126; EC 4.1.2.4; HMM-score: 288.5)
and 2 more
predicted phospho-2-dehydro-3-deoxyheptonate aldolase (TIGR01949; EC 4.2.1.-; HMM-score: 19.7)
heme/flavin dehydrogenase, mycofactocin system (TIGR03966; EC 1.-.-.-; HMM-score: 8.6)
TheSEED :
- Deoxyribose-phosphate aldolase (EC 4.1.2.4)
Carbohydrates Monosaccharides Deoxyribose and Deoxynucleoside Catabolism Deoxyribose-phosphate aldolase (EC 4.1.2.4)
⊞PFAM:
TIM_barrel (CL0036) DeoC; DeoC/LacD family aldolase (PF01791; HMM-score: 92.9)
and 4 more
His_biosynth; Histidine biosynthesis protein (PF00977; HMM-score: 16.5)
G3P_antiterm; Glycerol-3-phosphate responsive antiterminator (PF04309; HMM-score: 15.8)
no clan defined DAHP_snth_FXD; DAHP synthase ferredoxin-like domain (PF18152; HMM-score: 13.4)
6PGD_C (CL0106) UDPG_MGDP_dh; UDP-glucose/GDP-mannose dehydrogenase family, central domain (PF00984; HMM-score: 12.8)

⊟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
⊞
DeepLocPro: Cytoplasmic
- Cytoplasmic Score: 0.9986
- Cytoplasmic Membrane Score: 0.0002
- Cell wall & surface Score: 0
- Extracellular Score: 0.0012
⊞
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): 0.026807
- TAT(Tat/SPI): 0.000544
- LIPO(Sec/SPII): 0.001286
predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

GI: 88193913 NCBI
RefSeq: YP_498700 NCBI
UniProt: Q2G224 UniProt
STRING: 93061.SAOUHSC_00100 STRING

⊟Protein sequence[edit | edit source]

MKFEKYIDHTLLKPESTRTQIDQIIDEAKAYNFKSVCVNPTHVKYAAERLADSEVLVCTVIGFPLGASTTATKAFETEDAIQNGADEIDMVINIGALKDGRFDDVQQDIEAVVKAAKGHTVKVIIETVLLDHDEIVKASELTKAAGADFVKTSTGFAGGGATAEDVKLMKDTVGADVEVKASGGVRNLEDFNKMVEAGATRIGASAGVQIMQGLEADSDY

⊟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_01201	(acpP)	acyl carrier protein ^[4] (data from MRSA252)
SAOUHSC_02490	(adk)	adenylate kinase ^[4] (data from MRSA252)
SAOUHSC_01471	(asnC)	asparaginyl-tRNA synthetase ^[4] (data from MRSA252)
SAOUHSC_00790	(clpP)	ATP-dependent Clp protease proteolytic subunit ^[4] (data from MRSA252)
SAOUHSC_02380	(deoD)	purine nucleoside phosphorylase ^[4] (data from MRSA252)
SAOUHSC_01683	(dnaK)	molecular chaperone DnaK ^[4] (data from MRSA252)
SAOUHSC_00799	(eno)	phosphopyruvate hydratase ^[4] (data from MRSA252)
SAOUHSC_00574	(eutD)	phosphotransacetylase ^[4] (data from MRSA252)
SAOUHSC_02336	(fabZ)	(3R)-hydroxymyristoyl-ACP dehydratase ^[4] (data from MRSA252)
SAOUHSC_01236	(frr)	ribosome recycling factor ^[4] (data from MRSA252)
SAOUHSC_02117	(gatA)	aspartyl/glutamyl-tRNA amidotransferase subunit A ^[4] (data from MRSA252)
SAOUHSC_02116	(gatB)	aspartyl/glutamyl-tRNA amidotransferase subunit B ^[4] (data from MRSA252)
SAOUHSC_00375	(guaA)	GMP synthase ^[4] (data from MRSA252)
SAOUHSC_00225	(ispD)	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase ^[4] (data from MRSA252)
SAOUHSC_00493	(lysS)	lysyl-tRNA synthetase ^[4] (data from MRSA252)
SAOUHSC_01485	(ndk)	nucleoside diphosphate kinase ^[4] (data from MRSA252)
SAOUHSC_00900	(pgi)	glucose-6-phosphate isomerase ^[4] (data from MRSA252)
SAOUHSC_00796	(pgk)	phosphoglycerate kinase ^[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_02478	(rplM)	50S ribosomal protein L13 ^[4] (data from MRSA252)
SAOUHSC_02492	(rplO)	50S ribosomal protein L15 ^[4] (data from MRSA252)
SAOUHSC_01211	(rplS)	50S ribosomal protein L19 ^[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_01191	(rpmB)	50S ribosomal protein L28 ^[4] (data from MRSA252)
SAOUHSC_02493	(rpmD)	50S ribosomal protein L30 ^[4] (data from MRSA252)
SAOUHSC_01493	(rpsA)	30S ribosomal protein S1 ^[4] (data from MRSA252)
SAOUHSC_01232	(rpsB)	30S ribosomal protein S2 ^[4] (data from MRSA252)
SAOUHSC_02494	(rpsE)	30S ribosomal protein S5 ^[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_02487	(rpsM)	30S ribosomal protein S13 ^[4] (data from MRSA252)
SAOUHSC_01250	(rpsO)	30S ribosomal protein S15 ^[4] (data from MRSA252)
SAOUHSC_01208	(rpsP)	30S ribosomal protein S16 ^[4] (data from MRSA252)
SAOUHSC_00350	(rpsR)	30S ribosomal protein S18 ^[4] (data from MRSA252)
SAOUHSC_01689	(rpsT)	30S ribosomal protein S20 ^[4] (data from MRSA252)
SAOUHSC_01216	(sucC)	succinyl-CoA synthetase subunit beta ^[4] (data from MRSA252)
SAOUHSC_01779	(tig)	trigger factor ^[4] (data from MRSA252)
SAOUHSC_00797	(tpiA)	triosephosphate isomerase ^[4] (data from MRSA252)
SAOUHSC_01234	(tsf)	elongation factor Ts ^[4] (data from MRSA252)
SAOUHSC_02353	(upp)	uracil phosphoribosyltransferase ^[4] (data from MRSA252)
SAOUHSC_00002		DNA polymerase III subunit beta ^[4] (data from MRSA252)
SAOUHSC_00009		seryl-tRNA synthetase ^[4] (data from MRSA252)
SAOUHSC_00187		formate acetyltransferase ^[4] (data from MRSA252)
SAOUHSC_00336		acetyl-CoA acyltransferase ^[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_00499		pyridoxal biosynthesis lyase PdxS ^[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_00562		phosphomethylpyrimidine kinase ^[4] (data from MRSA252)
SAOUHSC_00634		ABC transporter substrate-binding protein ^[4] (data from MRSA252)
SAOUHSC_00679		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_00767		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_00795		glyceraldehyde-3-phosphate dehydrogenase ^[4] (data from MRSA252)
SAOUHSC_00878		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_00906		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_00937		oligoendopeptidase F ^[4] (data from MRSA252)
SAOUHSC_00951		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_01028		phosphocarrier protein HPr ^[4] (data from MRSA252)
SAOUHSC_01029		phosphoenolpyruvate-protein phosphotransferase ^[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_01100		thioredoxin ^[4] (data from MRSA252)
SAOUHSC_01150		cell division protein FtsZ ^[4] (data from MRSA252)
SAOUHSC_01199		3-oxoacyl-(acyl-carrier-protein) reductase ^[4] (data from MRSA252)
SAOUHSC_01218		succinyl-CoA synthetase subunit alpha ^[4] (data from MRSA252)
SAOUHSC_01287		glutamine synthetase ^[4] (data from MRSA252)
SAOUHSC_01327		catalase ^[4] (data from MRSA252)
SAOUHSC_01337		transketolase ^[4] (data from MRSA252)
SAOUHSC_01347		aconitate hydratase ^[4] (data from MRSA252)
SAOUHSC_01416		dihydrolipoamide succinyltransferase ^[4] (data from MRSA252)
SAOUHSC_01431		methionine sulfoxide reductase B ^[4] (data from MRSA252)
SAOUHSC_01451		threonine dehydratase ^[4] (data from MRSA252)
SAOUHSC_01632		glycine dehydrogenase subunit 2 ^[4] (data from MRSA252)
SAOUHSC_01666		glycyl-tRNA synthetase ^[4] (data from MRSA252)
SAOUHSC_01719		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_01806		pyruvate kinase ^[4] (data from MRSA252)
SAOUHSC_01807		6-phosphofructokinase ^[4] (data from MRSA252)
SAOUHSC_01814		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_01819		hypothetical protein ^[4] (data from MRSA252)
SAOUHSC_01820		acetate kinase ^[4] (data from MRSA252)
SAOUHSC_01901		putative translaldolase ^[4] (data from MRSA252)
SAOUHSC_01910		phosphoenolpyruvate carboxykinase ^[4] (data from MRSA252)
SAOUHSC_02108		ferritin ^[4] (data from MRSA252)
SAOUHSC_02366		fructose-bisphosphate aldolase ^[4] (data from MRSA252)
SAOUHSC_02369		DNA-directed RNA polymerase subunit delta ^[4] (data from MRSA252)
SAOUHSC_02377		pyrimidine-nucleoside phosphorylase ^[4] (data from MRSA252)
SAOUHSC_02379		2-deoxyribose-5-phosphate aldolase ^[4] (data from MRSA252)
SAOUHSC_02441		alkaline shock protein 23 ^[4] (data from MRSA252)
SAOUHSC_02486		30S ribosomal protein S11 ^[4] (data from MRSA252)
SAOUHSC_02830		D-lactate dehydrogenase ^[4] (data from MRSA252)
SAOUHSC_02860		HMG-CoA synthase ^[4] (data from MRSA252)
SAOUHSC_02869		1-pyrroline-5-carboxylate dehydrogenase ^[4] (data from MRSA252)
SAOUHSC_02926		fructose-1,6-bisphosphate aldolase ^[4] (data from MRSA252)
SAOUHSC_02927		malate:quinone oxidoreductase ^[4] (data from MRSA252)
SAOUHSC_02965		carbamate kinase ^[4] (data from MRSA252)
SAOUHSC_02968		ornithine carbamoyltransferase ^[4] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

MicrobesOnline: SAOUHSC_00097 > SAOUHSC_00099 > SAOUHSC_00100 > SAOUHSC_00101

⊟Regulation[edit | edit source]

regulator:

⊟Transcription pattern[edit | edit source]

S.aureus Expression Data Browser: ^[5] no expression profile plot available

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

Aureolib: data available for COL

⊟Protein stability[edit | edit source]

half-life: no data available

⊞Biological Material[edit | edit source]

⊞Other Information[edit | edit source]

⊟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)
↑ ^{Jump up to: 4.000} ^4.001 ^4.002 ^4.003 ^4.004 ^4.005 ^4.006 ^4.007 ^4.008 ^4.009 ^4.010 ^4.011 ^4.012 ^4.013 ^4.014 ^4.015 ^4.016 ^4.017 ^4.018 ^4.019 ^4.020 ^4.021 ^4.022 ^4.023 ^4.024 ^4.025 ^4.026 ^4.027 ^4.028 ^4.029 ^4.030 ^4.031 ^4.032 ^4.033 ^4.034 ^4.035 ^4.036 ^4.037 ^4.038 ^4.039 ^4.040 ^4.041 ^4.042 ^4.043 ^4.044 ^4.045 ^4.046 ^4.047 ^4.048 ^4.049 ^4.050 ^4.051 ^4.052 ^4.053 ^4.054 ^4.055 ^4.056 ^4.057 ^4.058 ^4.059 ^4.060 ^4.061 ^4.062 ^4.063 ^4.064 ^4.065 ^4.066 ^4.067 ^4.068 ^4.069 ^4.070 ^4.071 ^4.072 ^4.073 ^4.074 ^4.075 ^4.076 ^4.077 ^4.078 ^4.079 ^4.080 ^4.081 ^4.082 ^4.083 ^4.084 ^4.085 ^4.086 ^4.087 ^4.088 ^4.089 ^4.090 ^4.091 ^4.092 ^4.093 ^4.094 ^4.095 ^4.096 ^4.097 ^4.098 ^4.099 ^4.100 ^4.101 ^4.102 ^4.103 ^4.104 ^4.105 ^4.106 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)
↑ 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)

⊟Relevant publications[edit | edit source]

[pubmed19570206-1] 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)

[pubmed26224020-2] 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)

[pubmed28887440-3] 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)

[pubmed21166474-4] {Jump up to: 4.000} ^4.001 ^4.002 ^4.003 ^4.004 ^4.005 ^4.006 ^4.007 ^4.008 ^4.009 ^4.010 ^4.011 ^4.012 ^4.013 ^4.014 ^4.015 ^4.016 ^4.017 ^4.018 ^4.019 ^4.020 ^4.021 ^4.022 ^4.023 ^4.024 ^4.025 ^4.026 ^4.027 ^4.028 ^4.029 ^4.030 ^4.031 ^4.032 ^4.033 ^4.034 ^4.035 ^4.036 ^4.037 ^4.038 ^4.039 ^4.040 ^4.041 ^4.042 ^4.043 ^4.044 ^4.045 ^4.046 ^4.047 ^4.048 ^4.049 ^4.050 ^4.051 ^4.052 ^4.053 ^4.054 ^4.055 ^4.056 ^4.057 ^4.058 ^4.059 ^4.060 ^4.061 ^4.062 ^4.063 ^4.064 ^4.065 ^4.066 ^4.067 ^4.068 ^4.069 ^4.070 ^4.071 ^4.072 ^4.073 ^4.074 ^4.075 ^4.076 ^4.077 ^4.078 ^4.079 ^4.080 ^4.081 ^4.082 ^4.083 ^4.084 ^4.085 ^4.086 ^4.087 ^4.088 ^4.089 ^4.090 ^4.091 ^4.092 ^4.093 ^4.094 ^4.095 ^4.096 ^4.097 ^4.098 ^4.099 ^4.100 ^4.101 ^4.102 ^4.103 ^4.104 ^4.105 ^4.106 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)

[pubmed27035918-5] 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)

[1]

[2]

[3]

[4]

[5]

⊟Summary[edit | edit source]

Contents

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟DNA sequence[edit | edit source]

⊟Protein[edit | edit source]

⊟General[edit | edit source]

⊟Function[edit | edit source]

⊟Structure, modifications & cofactors[edit | edit source]

⊟Localization[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

⊟Experimental data[edit | edit source]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

⊞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]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]