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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1323 [new locus tag: SACOL_RS06740 ]
- pan locus tag?: SAUPAN003618000
- symbol: miaA
- pan gene symbol?: miaA
- synonym:
- product: tRNA delta(2)-isopentenylpyrophosphate transferase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1323 [new locus tag: SACOL_RS06740 ]
- symbol: miaA
- product: tRNA delta(2)-isopentenylpyrophosphate transferase
- replicon: chromosome
- strand: +
- coordinates: 1341464..1342399
- length: 936
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236397 NCBI
- RefSeq: YP_186178 NCBI
- BioCyc: see SACOL_RS06740
- MicrobesOnline: 912784 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGAATAAAAATAAGCCTTTTATTGTAGTAATTGTGGGGCCAACTGCTTCAGGTAAAACA
GAGCTTAGCATCGAACTCGCGAAGCGTATCAATGGTGAAATCATAAGCGGTGACTCTATG
CAAGTCTACAAACATATGAATATTGGAACTGCAAAAGTAACACCTGAAGAAATGGATGGT
ATTCCACATCATTTAATTGATATCTTGAATCCTGATGATACATTTTCAGCATATGAATTC
AAGCGATTAGCAGAAGATTTAATTACTGATATAACGAATAGAGGTAAAGTTCCAATCATA
GCAGGTGGAACAGGCTTATATATTCAATCATTAATATATAATTATGAATTAGAAGATGAA
ACAGTTACACCTGCACAATTATCCATAGTTAAACAAAAGTTATCTGCATTAGAACATTTA
GATAATCAGCAACTACACGATTATTTAGCTCAATTTGATGCGGTTTCTGCAGAAAATATT
CACCCTAACAACCGCCAAAGAGTGTTGCGCGCTATTGAATATTATTTAAAAACAAAAAAA
CTTTTGAGTAATCGCAAGAAAGTGCAACAATTTACTGAAAATTATGATACATTATTATTA
GGGATTGAAATGTCGCGTAAAACATTATATTCAAGAATAAATAAACGTGTTGATATTATG
TTGGATCACGGATTATTTAGAGAAGTGCAACAACTTGTTGAACAAGGCTATGAATCTTGC
CAAAGTATGCAAGCTATTGGATATAAAGAATTAATACCTGTGATTAACGGACAAATGATT
TATGAAGATGCTGTCAATGATTTAAAGCAACATTCACGCCAATATGCAAAACGACAAATG
ACATGGTTCAAGAATAAAATGAGTGTTCATTGGTTAGATAAAGAAAATATGTCACTTCAA
ATGATGTTAGATGAGATTACAACCCAGATTAAGTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1323 [new locus tag: SACOL_RS06740 ]
- symbol: MiaA
- description: tRNA delta(2)-isopentenylpyrophosphate transferase
- length: 311
- theoretical pI: 6.80558
- theoretical MW: 35868
- GRAVY: -0.431833
⊟Function[edit | edit source]
- reaction: EC 2.5.1.75? ExPASytRNA dimethylallyltransferase Dimethylallyl diphosphate + adenine37 in tRNA = diphosphate + N6-dimethylallyladenine37 in tRNA
- TIGRFAM: Protein synthesis tRNA and rRNA base modification tRNA dimethylallyltransferase (TIGR00174; EC 2.5.1.75; HMM-score: 324.5)and 4 morecarbohydrate kinase, thermoresistant glucokinase family (TIGR01313; EC 2.7.1.-; HMM-score: 15.3)Purines, pyrimidines, nucleosides, and nucleotides Nucleotide and nucleoside interconversions cytidylate kinase (TIGR00017; EC 2.7.4.14; HMM-score: 13.4)putative cytidylate kinase (TIGR02173; EC 2.7.4.14; HMM-score: 13.2)Central intermediary metabolism Other 2,4-diaminobutyrate 4-transaminase (TIGR00709; EC 2.6.1.-; HMM-score: 10.8)
- TheSEED :
- tRNA (adenine(37)-N(6))-dimethylallyltransferase (EC 2.5.1.75)
- PFAM: P-loop_NTPase (CL0023) IPPT; IPP transferase (PF01715; HMM-score: 267.1)and 7 moreIPT; Isopentenyl transferase (PF01745; HMM-score: 34.6)AAA_33; AAA domain (PF13671; HMM-score: 21.1)AAA_18; AAA domain (PF13238; HMM-score: 16.1)Zeta_toxin; Zeta toxin (PF06414; HMM-score: 14.5)RNA_helicase; RNA helicase (PF00910; HMM-score: 14.3)Cytidylate_kin; Cytidylate kinase (PF02224; HMM-score: 14.3)Hydin_ADK; Hydin Adenylate kinase-like domain (PF17213; HMM-score: 13.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: 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: 0.83
- Signal peptide possibility: -0.5
- N-terminally Anchored Score: -1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.071303
- TAT(Tat/SPI): 0.001764
- LIPO(Sec/SPII): 0.036275
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MNKNKPFIVVIVGPTASGKTELSIELAKRINGEIISGDSMQVYKHMNIGTAKVTPEEMDGIPHHLIDILNPDDTFSAYEFKRLAEDLITDITNRGKVPIIAGGTGLYIQSLIYNYELEDETVTPAQLSIVKQKLSALEHLDNQQLHDYLAQFDAVSAENIHPNNRQRVLRAIEYYLKTKKLLSNRKKVQQFTENYDTLLLGIEMSRKTLYSRINKRVDIMLDHGLFREVQQLVEQGYESCQSMQAIGYKELIPVINGQMIYEDAVNDLKQHSRQYAKRQMTWFKNKMSVHWLDKENMSLQMMLDEITTQIK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2]
- quantitative data / protein copy number per cell:
- interaction partners:
SACOL1062 (atl) bifunctional autolysin [3] (data from MRSA252) SACOL2095 (atpD) F0F1 ATP synthase subunit beta [3] (data from MRSA252) SACOL2253 (femX) femX protein [3] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [3] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [3] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [3] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SACOL0033 (mecA) penicillin-binding protein 2' [3] (data from MRSA252) SACOL1323 (miaA) tRNA delta(2)-isopentenylpyrophosphate transferase [3] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [3] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [3] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [3] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [3] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [3] (data from MRSA252) SACOL1277 (pyrH) uridylate kinase [3] (data from MRSA252) SACOL1536 (rluB) ribosomal large subunit pseudouridine synthase B [3] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SACOL2229 (rplN) 50S ribosomal protein L14 [3] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SACOL2223 (rplR) 50S ribosomal protein L18 [3] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SACOL2228 (rplX) 50S ribosomal protein L24 [3] (data from MRSA252) SACOL1700 (rpmA) 50S ribosomal protein L27 [3] (data from MRSA252) SACOL1238 (rpmB) 50S ribosomal protein L28 [3] (data from MRSA252) SACOL2231 (rpmC) 50S ribosomal protein L29 [3] (data from MRSA252) SACOL2112 (rpmE2) 50S ribosomal protein L31 [3] (data from MRSA252) SACOL1726 (rpmI) 50S ribosomal protein L35 [3] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [3] (data from MRSA252) SACOL0592 (rpsG) 30S ribosomal protein S7 [3] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [3] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [3] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [3] (data from MRSA252) SACOL1292 (rpsO) 30S ribosomal protein S15 [3] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [3] (data from MRSA252) SACOL0303 5'-nucleotidase [3] (data from MRSA252) SACOL0578 RNA methyltransferase [3] (data from MRSA252) SACOL0742 hypothetical protein [3] (data from MRSA252) SACOL0768 hypothetical protein [3] (data from MRSA252) SACOL0944 NADH dehydrogenase [3] (data from MRSA252) SACOL1294 metallo-beta-lactamase [3] (data from MRSA252) SACOL1426 hypothetical protein [3] (data from MRSA252) SACOL1615 DEAD/DEAH box helicase [3] (data from MRSA252) SACOL1651 hypothetical protein [3] (data from MRSA252) SACOL1753 universal stress protein [3] (data from MRSA252) SACOL1788 hypothetical protein [3] (data from MRSA252) SACOL1789 hypothetical protein [3] (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: 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) - ↑ 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) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 3.62 3.63 3.64 3.65 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)