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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL2213 [new locus tag: SACOL_RS11650 ]
- pan locus tag?: SAUPAN005676000
- symbol: rpoA
- pan gene symbol?: rpoA
- synonym:
- product: DNA-directed RNA polymerase subunit alpha
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL2213 [new locus tag: SACOL_RS11650 ]
- symbol: rpoA
- product: DNA-directed RNA polymerase subunit alpha
- replicon: chromosome
- strand: -
- coordinates: 2293956..2294900
- length: 945
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238614 NCBI
- RefSeq: YP_187023 NCBI
- BioCyc: see SACOL_RS11650
- MicrobesOnline: 913698 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGATAGAAATCGAAAAACCTAGAATTGAGACAATTGAAATTAGTGAAGATGCTAAATTC
GGTAAGTTCGTTGTTGAACCACTAGAACGTGGCTACGGTACTACACTAGGAAACTCCTTA
CGTCGTATCCTACTATCTTCATTACCAGGTGCAGCCGTTAAGTATATTGAAATTGAGGGA
GTTTTACATGAATTCTCAGCAGTAGACAATGTAGTTGAAGATGTTTCTACAATTATTATG
AACATTAAACAATTAGCATTGAAAATTTACTCTGAAGAAGATAAAACTTTAGAAATTGAT
GTACGTGATGAAGGCGAAGTAACAGCAAGCGACATTACACATGATAGTGATGTTGAAATT
TTAAACCCAGAGCTTAAAATTGCAACAGTATCTAAAGGTGGTCACTTAAAAATTCGTCTA
GTTGCTAACAAGGGTAGAGGTTACGCATTAGCAGAACAAAATAATACTAGTGATTTACCA
ATTGGTGTAATCCCTGTTGATTCATTGTATTCACCTGTTGAACGTGTGAACTATACTGTT
GAAAATACACGTGTAGGTCAAAGCAGTGATTTTGATAAATTAACATTGGATGTTTGGACT
AATGGTTCAATCACACCACAAGAATCAGTTTCATTAGCAGCAAAAATAATGACTGAACAC
TTGAATATCTTCGTTGGTCTTACTGATGAAGCGCAAAACGCTGAAATCATGATTGAAAAA
GAAGAAGATCAAAAAGAAAAAGTATTAGAAATGTCTATTGAAGAATTAGACTTATCTGTA
CGTTCATATAACTGCTTAAAACGCGCAGGAATCAATTCTGTTCAAGAGTTAGCTGACAAA
TCTGAAGCTGACATGATGAAAGTGCGTAATTTAGGTCGTAAATCTTTAGAAGAAGTTAAA
TACAAATTAGAAGATTTAGGATTAGGATTAAGAAAAGAAGATTGA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL2213 [new locus tag: SACOL_RS11650 ]
- symbol: RpoA
- description: DNA-directed RNA polymerase subunit alpha
- length: 314
- theoretical pI: 4.39431
- theoretical MW: 35011.5
- GRAVY: -0.302229
⊟Function[edit | edit source]
- reaction: EC 2.7.7.6? ExPASyDNA-directed RNA polymerase Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
- TIGRFAM: Transcription DNA-dependent RNA polymerase DNA-directed RNA polymerase, alpha subunit (TIGR02027; EC 2.7.7.6; HMM-score: 390.4)
- TheSEED :
- DNA-directed RNA polymerase alpha subunit (EC 2.7.7.6)
- PFAM: HHH (CL0198) RNA_pol_A_CTD; Bacterial RNA polymerase, alpha chain C terminal domain (PF03118; HMM-score: 98.7)RBP11-like (CL0509) RNA_pol_L; RNA polymerase Rpb3/Rpb11 dimerisation domain (PF01193; HMM-score: 84)no clan defined RNA_pol_A_bac; RNA polymerase Rpb3/RpoA insert domain (PF01000; HMM-score: 79.4)and 2 moreHHH (CL0198) HHH_5; Helix-hairpin-helix domain (PF14520; HMM-score: 14.7)no clan defined PASTA; PASTA domain (PF03793; HMM-score: 12.1)
⊟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): 0.007843
- TAT(Tat/SPI): 0.013642
- LIPO(Sec/SPII): 0.000555
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MIEIEKPRIETIEISEDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVKYIEIEGVLHEFSAVDNVVEDVSTIIMNIKQLALKIYSEEDKTLEIDVRDEGEVTASDITHDSDVEILNPELKIATVSKGGHLKIRLVANKGRGYALAEQNNTSDLPIGVIPVDSLYSPVERVNYTVENTRVGQSSDFDKLTLDVWTNGSITPQESVSLAAKIMTEHLNIFVGLTDEAQNAEIMIEKEEDQKEKVLEMSIEELDLSVRSYNCLKRAGINSVQELADKSEADMMKVRNLGRKSLEEVKYKLEDLGLGLRKED
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4]
- quantitative data / protein copy number per cell: 5325 [5]
- interaction partners:
SACOL2656 (arcB2) ornithine carbamoyltransferase [6] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [6] (data from MRSA252) SACOL1782 (fhs) formate--tetrahydrofolate ligase [6] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [6] (data from MRSA252) SACOL0593 (fusA) elongation factor G [6] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [6] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [6] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [6] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [6] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [6] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [6] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [6] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [6] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [6] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [6] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [6] (data from MRSA252) SACOL0839 (pgk) phosphoglycerate kinase [6] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [6] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [6] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [6] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [6] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [6] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [6] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [6] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [6] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [6] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [6] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [6] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [6] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [6] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [6] (data from MRSA252) SACOL1262 (sucC) succinyl-CoA synthetase subunit beta [6] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [6] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [6] (data from MRSA252) SACOL1759 universal stress protein [6] (data from MRSA252) SACOL2173 alkaline shock protein 23 [6] (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: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 26.91 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]
- ↑ 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) - ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 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) - ↑ 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)