From AureoWiki
Revision as of 08:44, 11 March 2016 by AureoSysAdmin (talk | contribs) (Text replacement - "* <aureodatabase>protein Genbank</aureodatabase> " to "")
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1118 [new locus tag: SACOL_RS05710 ]
  • pan locus tag?: SAUPAN003336000
  • symbol: typA
  • pan gene symbol?: typA
  • synonym:
  • product: GTP-binding protein TypA

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1118 [new locus tag: SACOL_RS05710 ]
  • symbol: typA
  • product: GTP-binding protein TypA
  • replicon: chromosome
  • strand: +
  • coordinates: 1127325..1129172
  • length: 1848
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    1681
    1741
    1801
    ATGACTAATAAAAGAGAAGATGTCCGCAATATAGCAATTATTGCTCACGTTGACCATGGT
    AAAACAACTTTAGTAGATGAGTTGTTAAAACAATCTGGTATATTCAGAGAAAATGAACAT
    GTCGATGAACGTGCAATGGACTCTAACGATATCGAAAGAGAGCGTGGAATTACGATTCTA
    GCCAAAAATACGGCTGTTGATTATAAAGGTACACGTATTAATATTTTGGATACACCAGGA
    CATGCAGACTTTGGTGGAGAAGTAGAACGTATTATGAAAATGGTTGATGGGGTTGTCTTA
    GTAGTAGATGCGTATGAAGGTACAATGCCTCAAACACGTTTTGTACTTAAAAAAGCGCTA
    GAACAAAACCTGAAACCTGTTGTTGTTGTTAATAAAATTGATAAACCATCAGCACGTCCA
    GAGGGTGTTGTAGATGAAGTTTTAGATTTATTTATTGAATTAGAAGCAAACGATGAACAA
    TTAGAATTCCCTGTTGTTTATGCTTCAGCAGTAAATGGTACAGCTAGCTTAGATCCTGAA
    AAGCAAGATGATAATTTACAATCATTATATGAAACAATTATTGATTATGTACCAGCTCCA
    ATTGATAACAGTGATGAGCCATTACAATTCCAAGTAGCATTGTTGGACTACAATGATTAT
    GTTGGACGTATTGGTATTGGTCGTGTATTCAGAGGTAAAATGCGTGTCGGAGATAATGTA
    TCACTAATTAAATTAGACGGTACAGTGAAAAACTTCCGTGTAACTAAAATCTTTGGTTAC
    TTTGGATTAAAACGTTTAGAAATTGAAGAAGCACAAGCTGGAGATTTAATTGCTGTTTCA
    GGTATGGAAGACATTAATGTTGGTGAAACTGTAACACCACATGACCATCAAGAAGCATTG
    CCAGTTCTACGTATTGATGAGCCTACTCTTGAAATGACATTTAAAGTTAACAATTCTCCA
    TTTGCTGGCCGTGAAGGTGACTTTGTAACAGCACGTCAAATTCAAGAACGTTTAAATCAA
    CAATTAGAAACAGATGTATCTTTGAAAGTTTCTAACACAGATTCTCCAGATACATGGGTA
    GTTGCTGGTCGCGGTGAATTGCATTTATCAATCCTTATTGAAAATATGCGTCGTGAAGGT
    TATGAATTACAAGTTTCAAAACCACAAGTAATTATTAAAGAAATAGATGGTGTAATGTGT
    GAACCATTTGAACGTGTGCAATGTGAAGTGCCACAAGAAAATGCAGGTGCTGTTATTGAA
    TCATTAGGTGCACGTAAAGGTGAAATGGTTGATATGACTACAACTGATAATGGACTTACA
    CGTTTAATCTTTAATGTACCGGCTCGTGGTATGATTGGTTATACGACTGAATTTATGTCA
    ATGACAAGAGGTTACGGTATTATTAACCATACATTTGAAGAATTTAGACCACGTATTAAA
    GCACAAATTGGCGGTCGTCGTAATGGTGCATTAATTTCAATGGATCAAGGTTCTGCAAGT
    ACTTATGCCATTTTGGGACTTGAAGATAGAGGTGTAAACTTCATGGAACCTGGTACTGAA
    GTTTATGAAGGTATGATTGTTGGTGAACATAATCGTGAAAATGATTTAACTGTTAACATC
    ACTAAAACAAAACATCAAACTAACGTACGTTCTGCAACGAAAGACCAAACACAAACAATG
    AATAGACCGCGTATTCTAACATTGGAAGAAGCGTTACAATTCATTAATGATGATGAACTT
    GTTGTGGTTACACCAGAAAGTATACGTTTAAGAAAGAAAATTTTAAACAAAAATGTTCGT
    GAAAAAGAAGCAAAGCGTATCAAACAAATGATGCAAGAAAACGAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740
    1800
    1848

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1118 [new locus tag: SACOL_RS05710 ]
  • symbol: TypA
  • description: GTP-binding protein TypA
  • length: 615
  • theoretical pI: 4.68551
  • theoretical MW: 69165
  • GRAVY: -0.405203

⊟Function[edit | edit source]

  • TIGRFAM:
    Cellular processes Cellular processes Adaptations to atypical conditions GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 939)
    Genetic information processing Protein synthesis Translation factors GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 939)
    Signal transduction Regulatory functions Other GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 939)
    and 18 more
    Genetic information processing Protein synthesis Translation factors translation elongation factor G (TIGR00484; HMM-score: 220.7)
    Genetic information processing Protein synthesis Translation factors translation elongation factor aEF-2 (TIGR00490; HMM-score: 217.2)
    Unknown function General elongation factor 4 (TIGR01393; EC 3.6.5.-; HMM-score: 209.7)
    Genetic information processing Protein synthesis Translation factors translation elongation factor Tu (TIGR00485; HMM-score: 100.1)
    Genetic information processing Protein synthesis Translation factors peptide chain release factor 3 (TIGR00503; HMM-score: 92.9)
    Unknown function General small GTP-binding protein domain (TIGR00231; HMM-score: 84.9)
    Genetic information processing Protein synthesis Translation factors selenocysteine-specific translation elongation factor (TIGR00475; HMM-score: 75.1)
    Genetic information processing Protein synthesis Translation factors translation initiation factor IF-2 (TIGR00487; HMM-score: 69.8)
    Genetic information processing Protein synthesis Translation factors translation elongation factor EF-1, subunit alpha (TIGR00483; HMM-score: 67.8)
    Metabolism Central intermediary metabolism Sulfur metabolism sulfate adenylyltransferase, large subunit (TIGR02034; EC 2.7.7.4; HMM-score: 48.7)
    Genetic information processing Protein synthesis Translation factors translation initiation factor aIF-2 (TIGR00491; HMM-score: 44.2)
    translation initiation factor 2, gamma subunit (TIGR03680; HMM-score: 39.8)
    Genetic information processing Protein synthesis Other ribosome-associated GTPase EngA (TIGR03594; HMM-score: 26.2)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA modification GTPase TrmE (TIGR00450; EC 3.6.-.-; HMM-score: 13.6)
    Genetic information processing Protein fate Protein modification and repair [FeFe] hydrogenase H-cluster maturation GTPase HydF (TIGR03918; HMM-score: 13.5)
    exopolysaccharide/PEP-CTERM locus tyrosine autokinase (TIGR03018; EC 2.7.10.2; HMM-score: 13.3)
    Genetic information processing Protein synthesis Other ribosome biogenesis GTP-binding protein YsxC (TIGR03598; HMM-score: 13)
    Metabolism Transport and binding proteins Cations and iron carrying compounds ferrous iron transport protein B (TIGR00437; HMM-score: 12.2)
  • TheSEED  :
    • GTP-binding protein TypA/BipA
    Protein Metabolism Protein biosynthesis Universal GTPases  GTP-binding protein TypA/BipA
  • PFAM:
    P-loop_NTPase (CL0023) GTP_EFTU; Elongation factor Tu GTP binding domain (PF00009; HMM-score: 193.4)
    and 10 more
    EF-G_C (CL0437) EFG_C; Elongation factor G C-terminus (PF00679; HMM-score: 78.6)
    EFTPs (CL0575) GTP_EFTU_D2; Elongation factor Tu domain 2 (PF03144; HMM-score: 41.2)
    P-loop_NTPase (CL0023) MMR_HSR1; 50S ribosome-binding GTPase (PF01926; HMM-score: 31.7)
    EF-G_C (CL0437) EFG_II; Elongation Factor G, domain II (PF14492; HMM-score: 30.2)
    P-loop_NTPase (CL0023) FeoB_N; Ferrous iron transport protein B (PF02421; HMM-score: 20.3)
    Arf; ADP-ribosylation factor family (PF00025; HMM-score: 19.8)
    Septin; Septin (PF00735; HMM-score: 17.4)
    Roc; Ras of Complex, Roc, domain of DAPkinase (PF08477; HMM-score: 13.6)
    SRPRB; Signal recognition particle receptor beta subunit (PF09439; HMM-score: 13.6)
    Ras; Ras family (PF00071; HMM-score: 12.2)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 1.05
    • Cytoplasmic Membrane Score: 8.78
    • Cellwall Score: 0.08
    • Extracellular Score: 0.09
    • 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): 0.002979
    • TAT(Tat/SPI): 0.000328
    • LIPO(Sec/SPII): 0.000462
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTNKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFPVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIKLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTPHDHQEALPVLRIDEPTLEMTFKVNNSPFAGREGDFVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRREGYELQVSKPQVIIKEIDGVMCEPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRPRIKAQIGGRRNGALISMDQGSASTYAILGLEDRGVNFMEPGTEVYEGMIVGEHNRENDLTVNITKTKHQTNVRSATKDQTQTMNRPRILTLEEALQFINDDELVVVTPESIRLRKKILNKNVREKEAKRIKQMMQENE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 444 [5]
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [6] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [6] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL2656(arcB2)ornithine carbamoyltransferase  [6] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [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)
    SACOL2016(groEL)chaperonin GroEL  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL0746(norR)MarR family transcriptional regulator  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [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)
    SACOL0841(pgm)phosphoglyceromutase  [6] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [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)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2221(rpmD)50S ribosomal protein L30  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL1254(rpsP)30S ribosomal protein S16  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [6] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0742hypothetical protein  [6] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL1952ferritins family protein  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 15.07 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. ↑ 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)
  2. ↑ 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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. ↑ 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 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 6.46 6.47 6.48 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)
  7. ↑ 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]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1118&oldid=92061"