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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1506 [new locus tag: SACOL_RS07670 ]
- pan locus tag?: SAUPAN003926000
- symbol: aroC
- pan gene symbol?: aroC
- synonym:
- product: chorismate synthase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1506 [new locus tag: SACOL_RS07670 ]
- symbol: aroC
- product: chorismate synthase
- replicon: chromosome
- strand: -
- coordinates: 1547075..1548241
- length: 1167
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237903 NCBI
- RefSeq: YP_186350 NCBI
- BioCyc: see SACOL_RS07670
- MicrobesOnline: 912958 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1141ATGAGATACCTAACATCAGGAGAATCACATGGACCTCAATTAACAGTTATTGTTGAAGGT
GTACCTGCAAATATAGAAATTAAGGTTGAGGATATTAATAAAGAAATGTTTAAGCGTCAA
GGCGGTTACGGACGTGGACGTCGTATGCAAATTGAGAAAGATACAGTAGAAATAGTATCA
GGCGTTAGAAATGGTTATACATTAGGTAGTCCAATTACTATGGTTGTAACCAATGATGAC
TTTACGCATTGGAGAAAAATTATGGGAGCAGCTCCAATAAGTGAAGAAGAACGTGAAAAT
ATGAAACGTACTATTACAAAACCAAGACCTGGTCATGCAGATTTGGTTGGAGGTATGAAA
TATAATCATCGTGATTTACGAAATGTGCTAGAGCGATCATCTGCTAGAGAAACAGCAGCT
CGAGTTGCAGTCGGTGCCTTATGTAAAGTGTTATTACAACAGTTAGATATCGATATATAC
AGTCGTGTTGTTGAAATAGGTGGAATTAAAGATAAAGATTTTTATGATTCAGAAACATTT
AAAGCAAATCTTGATCGTAATGATGTTCGTGTAATTGATGACAGTATCGCACAAGCAATG
CGAGATAAAATTGACGAAGCTAAAAATGAAGGAGATTCAATTGGCGGTGTCGTTCAAGTT
GTAGTTGAAAATATGCCTGTTGGTGTAGGTAGTTATGTGCATTATGATCGTAAGTTAGAT
GGTAAGATTGCACAAGGTGTTGTCAGCATAAATGCTTTTAAAGGTGTAAGCTTTGGTGAA
GGATTTAAAGCAGCTGAAAAGCCAGGTAGTGAGATTCAAGATGAAATTCTATATAATAGT
GAAATTGGTTATTATCGTGGATCTAATCACTTAGGTGGTTTAGAAGGCGGTATGTCAAAT
GGAATGCCAATTATCGTTAATGGTGTAATGAAACCAATTCCAACGTTATATAAACCATTA
AATTCAGTAGACATTAATACTAAAGAAGACTTTAAAGCAACAATTGAACGTTCTGATAGT
TGTGCTGTTCCTGCAGCAAGTATCGTCTGCGAACATGTCGTAGCATTTGAAATAGCAAAA
GCATTATTGGAAGAATTCCAATCAAATCATATTGAGCAACTTAAACAACAAATTATTGAG
CGCAGACAATTAAATATTGAGTTTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1506 [new locus tag: SACOL_RS07670 ]
- symbol: AroC
- description: chorismate synthase
- length: 388
- theoretical pI: 5.71849
- theoretical MW: 43046.6
- GRAVY: -0.363918
⊟Function[edit | edit source]
- reaction: EC 4.2.3.5? ExPASyChorismate synthase 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
- TIGRFAM: Amino acid biosynthesis Aromatic amino acid family chorismate synthase (TIGR00033; EC 4.2.3.5; HMM-score: 404.6)and 1 moreUnknown function Enzymes of unknown specificity archaeal radical SAM protein, PTO1314 family (TIGR03961; HMM-score: 12.6)
- TheSEED :
- Chorismate synthase (EC 4.2.3.5)
Amino Acids and Derivatives Aromatic amino acids and derivatives Chorismate Synthesis Chorismate synthase (EC 4.2.3.5)and 1 more - PFAM: no clan defined Chorismate_synt; Chorismate synthase (PF01264; HMM-score: 393.2)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: FMNH2
- 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): 0.017486
- TAT(Tat/SPI): 0.00073
- LIPO(Sec/SPII): 0.00203
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MRYLTSGESHGPQLTVIVEGVPANIEIKVEDINKEMFKRQGGYGRGRRMQIEKDTVEIVSGVRNGYTLGSPITMVVTNDDFTHWRKIMGAAPISEEERENMKRTITKPRPGHADLVGGMKYNHRDLRNVLERSSARETAARVAVGALCKVLLQQLDIDIYSRVVEIGGIKDKDFYDSETFKANLDRNDVRVIDDSIAQAMRDKIDEAKNEGDSIGGVVQVVVENMPVGVGSYVHYDRKLDGKIAQGVVSINAFKGVSFGEGFKAAEKPGSEIQDEILYNSEIGYYRGSNHLGGLEGGMSNGMPIIVNGVMKPIPTLYKPLNSVDINTKEDFKATIERSDSCAVPAASIVCEHVVAFEIAKALLEEFQSNHIEQLKQQIIERRQLNIEF
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 248 [4]
- interaction partners:
SACOL1760 (ackA) acetate kinase [5] (data from MRSA252) SACOL1385 (acnA) aconitate hydratase [5] (data from MRSA252) SACOL1494 (asnC) asparaginyl-tRNA synthetase [5] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [5] (data from MRSA252) SACOL0002 (dnaN) DNA polymerase III subunit beta [5] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [5] (data from MRSA252) SACOL0634 (eutD) phosphotransacetylase [5] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [5] (data from MRSA252) SACOL2091 (fabZ) (3R)-hydroxymyristoyl-ACP dehydratase [5] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [5] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [5] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [5] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [5] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [5] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [5] (data from MRSA252) SACOL1477 (ilvA1) threonine dehydratase [5] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [5] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [5] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [5] (data from MRSA252) SACOL2618 (ldh2) L-lactate dehydrogenase [5] (data from MRSA252) SACOL1054 (menB) naphthoate synthase [5] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [5] (data from MRSA252) SACOL0792 (nrdE) ribonucleotide-diphosphate reductase subunit alpha [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [5] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0839 (pgk) phosphoglycerate kinase [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [5] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [5] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [5] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [5] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [5] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [5] (data from MRSA252) SACOL2207 (rplM) 50S ribosomal protein L13 [5] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [5] (data from MRSA252) SACOL2212 (rplQ) 50S ribosomal protein L17 [5] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [5] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [5] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [5] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL2228 (rplX) 50S ribosomal protein L24 [5] (data from MRSA252) SACOL0545 (rplY) 50S ribosomal protein L25/general stress protein Ctc [5] (data from MRSA252) SACOL1700 (rpmA) 50S ribosomal protein L27 [5] (data from MRSA252) SACOL2231 (rpmC) 50S ribosomal protein L29 [5] (data from MRSA252) SACOL2112 (rpmE2) 50S ribosomal protein L31 [5] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [5] (data from MRSA252) SACOL1516 (rpsA) 30S ribosomal protein S1 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [5] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [5] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [5] (data from MRSA252) SACOL1292 (rpsO) 30S ribosomal protein S15 [5] (data from MRSA252) SACOL1254 (rpsP) 30S ribosomal protein S16 [5] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [5] (data from MRSA252) SACOL0439 (rpsR) 30S ribosomal protein S18 [5] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [5] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [5] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [5] (data from MRSA252) SACOL1263 (sucD) succinyl-CoA synthetase subunit alpha [5] (data from MRSA252) SACOL0915 (sufD) FeS assembly protein SufD [5] (data from MRSA252) SACOL1722 (tig) trigger factor [5] (data from MRSA252) SACOL1377 (tkt) transketolase [5] (data from MRSA252) SACOL0840 (tpiA) triosephosphate isomerase [5] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL2104 (upp) uracil phosphoribosyltransferase [5] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0815 ribosomal subunit interface protein [5] (data from MRSA252) SACOL0914 FeS assembly ATPase SufC [5] (data from MRSA252) SACOL0931 HAD superfamily hydrolase [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [5] (data from MRSA252) SACOL1098 hypothetical protein [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252) SACOL1952 ferritins family protein [5] (data from MRSA252) SACOL2114 aldehyde dehydrogenase [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: CodY (repression) regulon
CodY (TF) important in Amino acid metabolism; 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: 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]
- ↑ 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, 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) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 5.51 5.52 5.53 5.54 5.55 5.56 5.57 5.58 5.59 5.60 5.61 5.62 5.63 5.64 5.65 5.66 5.67 5.68 5.69 5.70 5.71 5.72 5.73 5.74 5.75 5.76 5.77 5.78 5.79 5.80 5.81 5.82 5.83 5.84 5.85 5.86 5.87 5.88 5.89 5.90 5.91 5.92 5.93 5.94 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)