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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1745 [new locus tag: SACOL_RS08930 ]
- pan locus tag?: SAUPAN004324000
- symbol: pyk
- pan gene symbol?: pykA
- synonym:
- product: pyruvate kinase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1745 [new locus tag: SACOL_RS08930 ]
- symbol: pyk
- product: pyruvate kinase
- replicon: chromosome
- strand: -
- coordinates: 1781926..1783683
- length: 1758
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238347 NCBI
- RefSeq: YP_186581 NCBI
- BioCyc: see SACOL_RS08930
- MicrobesOnline: 913191 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1741ATGAGAAAAACTAAAATTGTATGTACAATTGGACCAGCTTCAGAATCAGAAGAAATGATT
GAGAAATTAATCAATGCTGGTATGAACGTTGCACGATTAAACTTTTCACATGGTAGTCAT
GAAGAGCATAAAGGTAGAATTGATACAATTCGTAAAGTAGCTAAAAGATTAGACAAAATT
GTAGCAATTTTATTAGATACAAAAGGTCCAGAAATTCGTACGCATAATATGAAAGACGGT
ATCATTGAACTTGAACGTGGCAACGAAGTTATTGTTAGCATGAATGAAGTTGAAGGAACA
CCTGAAAAGTTCTCAGTAACATATGAAAACTTAATTAACGATGTTCAAGTAGGTTCATAC
ATTTTACTTGATGATGGCTTAATTGAATTACAAGTTAAAGATATTGACCATGCTAAAAAA
GAAGTTAAATGTGATATTTTAAACTCTGGTGAGCTTAAAAACAAAAAAGGTGTTAACTTA
CCTGGCGTAAGAGTAAGTTTACCTGGTATTACAGAAAAAGATGCTGAAGATATCCGTTTC
GGTATTAAAGAAAATGTTGACTTCATTGCAGCAAGTTTCGTACGTCGTCCTAGTGATGTT
TTAGAAATTCGTGAAATTTTAGAAGAACAAAAAGCTAACATTTCAGTATTCCCTAAAATT
GAAAACCAAGAAGGTATTGATAATATTGCGGAAATTCTTGAAGTGTCTGATGGTTTAATG
GTTGCACGTGGTGACATGGGTGTTGAAATTCCACCTGAAAAAGTACCAATGGTTCAAAAA
GATTTAATCAGACAATGTAACAAATTAGGTAAACCAGTTATTACAGCTACACAAATGTTA
GATTCTATGCAACGTAACCCACGTGCTACACGTGCAGAAGCTAGTGACGTTGCCAACGCA
ATCTATGATGGTACAGATGCAGTAATGTTATCTGGTGAAACTGCTGCTGGTTTATATCCT
GAAGAAGCTGTTAAAACAATGAGAAATATTGCTGTATCAGCTGAAGCAGCCCAAGATTAC
AAAAAGTTATTGTCAGATCGTACTAAATTAGTTGAAACTTCATTAGTGAATGCTATCGGT
ATTTCGGTTGCACATACAGCTTTAAACTTAAATGTTAAAGCAATTGTAGCTGCTACTGAA
AGTGGTTCAACGGCACGTACTATCTCCAAATATCGTCCACATTCAGACATTATTGCGGTG
ACTCCAAGTGAAGAAACTGCACGTCAATGTTCAATTGTTTGGGGAGTTCAACCTGTAGTT
AAAAAAGGACGTAAGAGTACAGATGCATTGTTAAACAATGCAGTTGCAACAGCTGTTGAA
ACTGGTAGAGTATCTAATGGTGATTTAATCATTATTACTGCTGGTGTACCAACTGGTGAA
ACTGGAACTACTAATATGATGAAAATCCACCTAGTTGGTGACGAAATTGCTAATGGTCAA
GGTATTGGACGTGGATCAGTTGTTGGTACTACGTTAGTTGCTGAAACTGTTAAAGATTTA
GAAGGTAAAGATTTATCTGACAAAGTTATCGTTACTAACTCAATCGATGAAACGTTTGTA
CCTTATGTAGAAAAAGCTTTAGGCTTAATTACAGAAGAAAATGGTATTACATCACCAAGT
GCAATTGTTGGTTTAGAAAAAGGTATTCCAACAGTTGTAGGTGTAGAAAAAGCTGTTAAA
AACATAAGCAATAACATGTTAGTTACGATTGATGCTGCTCAAGGTAAAATCTTTGAAGGA
TATGCAAACGTACTATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1745 [new locus tag: SACOL_RS08930 ]
- symbol: Pyk
- description: pyruvate kinase
- length: 585
- theoretical pI: 4.99555
- theoretical MW: 63101.9
- GRAVY: -0.127863
⊟Function[edit | edit source]
- reaction: EC 2.7.1.40? ExPASyPyruvate kinase ATP + pyruvate = ADP + phosphoenolpyruvate
- TIGRFAM: Energy metabolism Glycolysis/gluconeogenesis pyruvate kinase (TIGR01064; EC 2.7.1.40; HMM-score: 619.1)and 4 moreEnergy metabolism Glycolysis/gluconeogenesis phosphoenolpyruvate synthase (TIGR01418; EC 2.7.9.2; HMM-score: 56.3)phosphoenolpyruvate-protein phosphotransferase (TIGR01417; EC 2.7.3.9; HMM-score: 27.2)2-dehydro-3-deoxyglucarate aldolase (TIGR03239; EC 4.1.2.20; HMM-score: 15.6)2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase (TIGR02311; EC 4.1.2.-; HMM-score: 14.4)
- TheSEED :
- Phosphohistidine swiveling domain
- Pyruvate kinase (EC 2.7.1.40)
Carbohydrates Central carbohydrate metabolism Glycolysis and Gluconeogenesis Pyruvate kinase (EC 2.7.1.40)and 3 more - PFAM: PK_TIM (CL0151) PK; Pyruvate kinase, barrel domain (PF00224; HMM-score: 511.6)and 4 moreno clan defined PK_C; Pyruvate kinase, alpha/beta domain (PF02887; HMM-score: 127.9)Leu-IlvD (CL0364) PEP-utilizers; PEP-utilising enzyme, mobile domain (PF00391; HMM-score: 55.7)HTH (CL0123) IF2_N; Translation initiation factor IF-2, N-terminal region (PF04760; HMM-score: 19)PK_TIM (CL0151) HpcH_HpaI; HpcH/HpaI aldolase/citrate lyase family (PF03328; HMM-score: 14.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: K+, Mg2+
- 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: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.012748
- TAT(Tat/SPI): 0.000555
- LIPO(Sec/SPII): 0.001816
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MRKTKIVCTIGPASESEEMIEKLINAGMNVARLNFSHGSHEEHKGRIDTIRKVAKRLDKIVAILLDTKGPEIRTHNMKDGIIELERGNEVIVSMNEVEGTPEKFSVTYENLINDVQVGSYILLDDGLIELQVKDIDHAKKEVKCDILNSGELKNKKGVNLPGVRVSLPGITEKDAEDIRFGIKENVDFIAASFVRRPSDVLEIREILEEQKANISVFPKIENQEGIDNIAEILEVSDGLMVARGDMGVEIPPEKVPMVQKDLIRQCNKLGKPVITATQMLDSMQRNPRATRAEASDVANAIYDGTDAVMLSGETAAGLYPEEAVKTMRNIAVSAEAAQDYKKLLSDRTKLVETSLVNAIGISVAHTALNLNVKAIVAATESGSTARTISKYRPHSDIIAVTPSEETARQCSIVWGVQPVVKKGRKSTDALLNNAVATAVETGRVSNGDLIIITAGVPTGETGTTNMMKIHLVGDEIANGQGIGRGSVVGTTLVAETVKDLEGKDLSDKVIVTNSIDETFVPYVEKALGLITEENGITSPSAIVGLEKGIPTVVGVEKAVKNISNNMLVTIDAAQGKIFEGYANVL
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3] [4] [5]
- quantitative data / protein copy number per cell: 4298 [6]
- interaction partners:
SACOL1760 (ackA) acetate kinase [7] (data from MRSA252) SACOL1385 (acnA) aconitate hydratase [7] (data from MRSA252) SACOL0660 (adhP) alcohol dehydrogenase [7] (data from MRSA252) SACOL0451 (ahpF) alkyl hydroperoxide reductase subunit F [7] (data from MRSA252) SACOL1478 (ald1) alanine dehydrogenase [7] (data from MRSA252) SACOL2657 (arcA) arginine deiminase [7] (data from MRSA252) SACOL2656 (arcB2) ornithine carbamoyltransferase [7] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [7] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [7] (data from MRSA252) SACOL1587 (efp) elongation factor P [7] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [7] (data from MRSA252) SACOL0634 (eutD) phosphotransacetylase [7] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [7] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [7] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [7] (data from MRSA252) SACOL0593 (fusA) elongation factor G [7] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [7] (data from MRSA252) SACOL0877 (gcvH) glycine cleavage system protein H [7] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [7] (data from MRSA252) SACOL1554 (gnd) 6-phosphogluconate dehydrogenase [7] (data from MRSA252) SACOL0461 (guaA) GMP synthase [7] (data from MRSA252) SACOL0460 (guaB) inosine-5'-monophosphate dehydrogenase [7] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [7] (data from MRSA252) SACOL1477 (ilvA1) threonine dehydratase [7] (data from MRSA252) SACOL2618 (ldh2) L-lactate dehydrogenase [7] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [7] (data from MRSA252) SACOL0792 (nrdE) ribonucleotide-diphosphate reductase subunit alpha [7] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [7] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [7] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [7] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [7] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [7] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [7] (data from MRSA252) SACOL0839 (pgk) phosphoglycerate kinase [7] (data from MRSA252) SACOL1091 (ptsH) phosphocarrier protein HPr [7] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [7] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [7] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [7] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [7] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [7] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [7] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [7] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [7] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [7] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [7] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [7] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [7] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [7] (data from MRSA252) SACOL0545 (rplY) 50S ribosomal protein L25/general stress protein Ctc [7] (data from MRSA252) SACOL2213 (rpoA) DNA-directed RNA polymerase subunit alpha [7] (data from MRSA252) SACOL0588 (rpoB) DNA-directed RNA polymerase subunit beta [7] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [7] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [7] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [7] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [7] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [7] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [7] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [7] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [7] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [7] (data from MRSA252) SACOL0009 (serS) seryl-tRNA synthetase [7] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [7] (data from MRSA252) SACOL1262 (sucC) succinyl-CoA synthetase subunit beta [7] (data from MRSA252) SACOL1722 (tig) trigger factor [7] (data from MRSA252) SACOL0840 (tpiA) triosephosphate isomerase [7] (data from MRSA252) SACOL1155 (trxA) thioredoxin [7] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [7] (data from MRSA252) SACOL0521 hypothetical protein [7] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [7] (data from MRSA252) SACOL0815 ribosomal subunit interface protein [7] (data from MRSA252) SACOL1020 hypothetical protein [7] (data from MRSA252) SACOL1437 CSD family cold shock protein [7] (data from MRSA252) SACOL1759 universal stress protein [7] (data from MRSA252) SACOL1952 ferritins family protein [7] (data from MRSA252) SACOL2173 alkaline shock protein 23 [7] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [7] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: CcpA regulon
CcpA (TF) important in Carbon catabolism; RegPrecise transcription unit transferred from N315 data 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: 58.55 h [8]
⊟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) - ↑ Annette Dreisbach, Kristina Hempel, Girbe Buist, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
Profiling the surfacome of Staphylococcus aureus.
Proteomics: 2010, 10(17);3082-96
[PubMed:20662103] [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) - ↑ 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 7.11 7.12 7.13 7.14 7.15 7.16 7.17 7.18 7.19 7.20 7.21 7.22 7.23 7.24 7.25 7.26 7.27 7.28 7.29 7.30 7.31 7.32 7.33 7.34 7.35 7.36 7.37 7.38 7.39 7.40 7.41 7.42 7.43 7.44 7.45 7.46 7.47 7.48 7.49 7.50 7.51 7.52 7.53 7.54 7.55 7.56 7.57 7.58 7.59 7.60 7.61 7.62 7.63 7.64 7.65 7.66 7.67 7.68 7.69 7.70 7.71 7.72 7.73 7.74 7.75 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)