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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0452 [new locus tag: SACOL_RS02285 ]
- pan locus tag?: SAUPAN001982000
- symbol: ahpC
- pan gene symbol?: ahpC
- synonym:
- product: alkyl hydroperoxide reductase subunit C
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0452 [new locus tag: SACOL_RS02285 ]
- symbol: ahpC
- product: alkyl hydroperoxide reductase subunit C
- replicon: chromosome
- strand: -
- coordinates: 453332..453901
- length: 570
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236480 NCBI
- RefSeq: YP_185342 NCBI
- BioCyc:
- MicrobesOnline: 911922 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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541ATGTCATTAATTAACAAAGAAATCTTACCATTTACAGCGCAAGCTTTCGATCCAAAAAAA
GATCAATTTAAAGAAGTTACACAAGAAGATTTAAAAGGTTCTTGGAGCGTAGTATGCTTC
TATCCTGCTGACTTCTCATTCGTTTGTCCAACTGAATTAGAAGACTTACAAAACCAATAT
GAAGAATTACAAAAATTAGGCGTAAATGTATTCTCAGTATCAACTGATACTCACTTCGTA
CACAAAGCATGGCATGACCATTCAGATGCAATTAGCAAAATCACTTACACTATGATTGGT
GACCCATCACAAACAATCACTCGTAATTTTGATGTATTAGATGAAGCTACTGGTTTAGCT
CAACGTGGTACATTCATTATCGACCCAGACGGTGTTGTACAAGCATCTGAAATTAACGCT
GACGGAATTGGCCGTGACGCTAGTACATTAGCTCACAAAATCAAAGCAGCTCAATATGTT
CGTAAAAACCCTGGCGAAGTATGCCCAGCTAAATGGGAAGAAGGCGCTAAAACATTGCAA
CCTGGTTTAGATTTAGTAGGTAAAATCTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0452 [new locus tag: SACOL_RS02285 ]
- symbol: AhpC
- description: alkyl hydroperoxide reductase subunit C
- length: 189
- theoretical pI: 4.6567
- theoretical MW: 20976.5
- GRAVY: -0.331217
⊟Function[edit | edit source]
- reaction: EC 1.11.1.15? ExPASyPeroxiredoxin 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
- TIGRFAM: Cellular processes Detoxification peroxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)Cellular processes Adaptations to atypical conditions peroxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)
- TheSEED:
- PFAM: Thioredoxin (CL0172) AhpC-TSA; AhpC/TSA family (PF00578; HMM-score: 119.2)and 4 moreRedoxin; Redoxin (PF08534; HMM-score: 52.2)no clan defined 1-cysPrx_C; C-terminal domain of 1-Cys peroxiredoxin (PF10417; HMM-score: 25)Thioredoxin (CL0172) SCO1-SenC; SCO1/SenC (PF02630; HMM-score: 21.2)Glyco_hydro_tim (CL0058) NAGidase; beta-N-acetylglucosaminidase (PF07555; HMM-score: 12.6)
⊟Structure, modifications & interactions[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
- protein partners:
SACOL2657 (arcA) arginine deiminase [1] (data from MRSA252) SACOL1215 (carB) carbamoyl phosphate synthase large subunit [1] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [1] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [1] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [1] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [1] (data from MRSA252) SACOL2016 (groEL) chaperonin GroEL [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [1] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [1] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [1] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [1] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [1] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [1] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [1] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [1] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [1] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [1] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [1] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [1] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [1] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [1] (data from MRSA252) SACOL2213 (rpoA) DNA-directed RNA polymerase subunit alpha [1] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [1] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [1] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [1] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [1] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [1] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [1] (data from MRSA252) SACOL0944 NADH dehydrogenase [1] (data from MRSA252) SACOL1759 universal stress protein [1] (data from MRSA252) SACOL2173 alkaline shock protein 23 [1] (data from MRSA252) SACOL2553 pyruvate oxidase [1] (data from MRSA252)
⊟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: 0
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.012719
- TAT(Tat/SPI): 0.000229
- LIPO(Sec/SPII): 0.000739
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MSLINKEILPFTAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGEVCPAKWEEGAKTLQPGLDLVGKI
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlasquantitative data / protein copy number per cell: 12844 [6]
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: PerR* (repression) regulon
PerR (TF) important in Oxidative stress response; RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 17.58 h [7]
⊟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]
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 1.43 1.44 1.45 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) - ↑ 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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
J Proteome Res: 2010, 9(3);1579-90
[PubMed:20108986] [WorldCat.org] [DOI] (I p) - ↑ 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)
⊟Relevant publications[edit | edit source]