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PangenomeCOLN315NCTC8325NewmanUSA300_FPR375704-0298108BA0217611819-97685071193ECT-R 2ED133ED98HO 5096 0412JH1JH9JKD6008JKD6159JSNZLGA251M013MRSA252MSHR1132MSSA476MW2Mu3Mu50RF122ST398T0131TCH60TW20USA300_TCH1516VC40

NCBI: 03-AUG-2016

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⊟Summary[edit | edit source]

Contents

  • 1 Summary
  • 2 Genome View
  • 3 Gene
    • 3.1 General
    • 3.2 Accession numbers
    • 3.3 Phenotype
    • 3.4 DNA sequence
  • 4 Protein
    • 4.1 General
    • 4.2 Function
    • 4.3 Structure, modifications & cofactors
    • 4.4 Localization
    • 4.5 Accession numbers
    • 4.6 Protein sequence
    • 4.7 Experimental data
  • 5 Expression & Regulation
    • 5.1 Operon
    • 5.2 Regulation
    • 5.3 Transcription pattern
    • 5.4 Protein synthesis (provided by Aureolib)
    • 5.5 Protein stability
  • 6 Biological Material
    • 6.1 Mutants
    • 6.2 Expression vector
    • 6.3 lacZ fusion
    • 6.4 GFP fusion
    • 6.5 two-hybrid system
    • 6.6 FLAG-tag construct
    • 6.7 Antibody
  • 7 Other Information
  • 8 Literature
    • 8.1 References
    • 8.2 Relevant publications
  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01838
  • pan locus tag?: SAUPAN004387000
  • symbol: SAOUHSC_01838
  • pan gene symbol?: htrA1
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01838
  • symbol: SAOUHSC_01838
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 1743299..1744573
  • length: 1275
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

  • Gene ID: 3921788 NCBI
  • RefSeq: YP_500344 NCBI
  • BioCyc: G1I0R-1710 BioCyc
  • MicrobesOnline: 1290258 MicrobesOnline

⊟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
    ATGTCAGATTTTAATCATACAGATCATTCTACAACAAACCATAGCCAAACACCTAGATAC
    AGAAGACCTAAATTTCCATGGTTTAAAACAGTCATCGTTGCATTGATTGCTGGAATTATT
    GGTGCACTTCTAGTACTTGGTATAGGCAAAGTATTAAATAGTACAATTTTAAATAAAGAT
    GGTTCAACTGTTCAGACAACAAATAATAAAGGTGGCAATCAATTAGACGGTCAAAGCAAG
    AAATTCGGTACCGTTCATGAAATGATAAAATCTGTCTCCCCTACAATTGTTGGAGTTATT
    AACATGCAAAAAGCATCAAGTGTAGACGACTTATTAAAAGGCAAATCATCTAAACCATCT
    GAAGCTGGAGTAGGTTCAGGTGTTATCTATCAAATAAACAACAATTCAGCTTATATCGTT
    ACAAACAATCATGTTATTGATGGCGCAAATGAAATTAGAGTCCAATTACATAATAAAAAA
    CAAGTTAAAGCGAAATTAGTTGGTAAAGATGCAGTAACTGATATTGCTGTACTTAAAATT
    GAAAATACAAAAGGTATTAAAGCGATTCAATTTGCCAACTCTTCAAAAGTACAAACTGGC
    GATAGCGTATTCGCAATGGGTAACCCATTAGGATTACAATTTGCTAACTCTGTAACATCT
    GGTATCATTTCAGCAAGCGAACGTACGATTGACGCTGAGACAACTGGTGGCAATACAAAA
    GTTAGCGTTCTTCAAACAGATGCTGCTATTAACCCAGGTAACTCAGGTGGCGCATTAGTA
    GATATTAATGGTAATTTAGTTGGTATTAACTCAATGAAAATTGCTGCGACACAAGTTGAA
    GGTATCGGGTTTGCTATTCCAAGTAATGAAGTTAAAGTAACAATTGAACAACTTGTAAAA
    CATGGTAAAATTGACCGCCCTTCGATTGGTATTGGTTTAATTAATTTGAAAGATATTCCT
    GAAGAAGAGCGCGAGCAACTTCATACTGATAGAGAAGACGGTATTTATGTCGCCAAAGCT
    GATAGTGATATTGATCTTAAAAAAGGTGATATTATTACAGAAATTGATGGCAAGAAAATT
    AAAGATGATGTTGATTTAAGAAGCTATTTATATGAAAATAAAAAACCTGGTGAATCAGTC
    ACTGTTACCGTTATCCGTGATGGTAAAACAAAAGAAGTTAAAGTGAAATTAAAACAACAA
    AAAGAACAACCAAAACGTCAAAGCCGATCAGAACGTCAATCACCTGGCCAAGGCGATAGA
    GATTTCTTTAGATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1275

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_01838
  • symbol: SAOUHSC_01838
  • description: hypothetical protein
  • length: 424
  • theoretical pI: 9.97226
  • theoretical MW: 45802.6
  • GRAVY: -0.416981

⊟Function[edit | edit source]

  • ⊞TIGRFAM:
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides peptidase Do (TIGR02037; EC 3.4.21.-; HMM-score: 291.6)
    Genetic information processing Protein fate Protein folding and stabilization peptidase Do (TIGR02037; EC 3.4.21.-; HMM-score: 291.6)
    and 4 more
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides periplasmic serine peptidase DegS (TIGR02038; EC 3.4.21.-; HMM-score: 182.6)
    Signal transduction Regulatory functions Protein interactions periplasmic serine peptidase DegS (TIGR02038; EC 3.4.21.-; HMM-score: 182.6)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides RIP metalloprotease RseP (TIGR00054; EC 3.4.24.-; HMM-score: 19)
    Genetic information processing Protein fate Protein and peptide secretion and trafficking type II secretion system protein C (TIGR01713; HMM-score: 16.6)
  • TheSEED  :
    • Serine protease Do-like HtrA (EC 3.4.21.107)
  • ⊞PFAM:
    Peptidase_PA (CL0124) Trypsin_2; Trypsin-like peptidase domain (PF13365; HMM-score: 116)
    and 7 more
    Trypsin; Trypsin (PF00089; HMM-score: 69.7)
    PDZ-like (CL0466) PDZ_2; PDZ domain (PF13180; HMM-score: 63.7)
    PDZ_6; PDZ domain (PF17820; HMM-score: 24.2)
    PDZ_Tricorn; Tricorn protease PDZ domain (PF14685; HMM-score: 22.6)
    Peptidase_PA (CL0124) Peptidase_S32; Equine arteritis virus serine endopeptidase S32 (PF05579; HMM-score: 17)
    Mycop_pep_DUF31; Mycoplasma peptidase (DUF31) (PF01732; HMM-score: 16.6)
    PDZ-like (CL0466) PDZ; PDZ domain (PF00595; HMM-score: 16.1)

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

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

⊟Localization[edit | edit source]

  • ⊞PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 0.32
    • Cytoplasmic Membrane Score: 9.55
    • Cellwall Score: 0.12
    • Extracellular Score: 0.01
    • Internal Helix: 1
  • ⊞DeepLocPro: Cytoplasmic Membrane
    • Cytoplasmic Score: 0.0002
    • Cytoplasmic Membrane Score: 0.9702
    • Cell wall & surface Score: 0.0045
    • Extracellular Score: 0.0252
  • ⊞LocateP: N-terminally anchored (No CS)
    • Prediction by SwissProt Classification: Membrane
    • Pathway Prediction: Sec-(SPI)
    • Intracellular possibility: 0.17
    • Signal peptide possibility: -0.5
    • N-terminally Anchored Score: 7
    • Predicted Cleavage Site: No CleavageSite
  • ⊞SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.023768
    • TAT(Tat/SPI): 0.001027
    • LIPO(Sec/SPII): 0.005047
  • predicted transmembrane helices (TMHMM): 1

⊟Accession numbers[edit | edit source]

  • GI: 88195538 NCBI
  • RefSeq: YP_500344 NCBI
  • UniProt: Q2FXJ6 UniProt
  • STRING: 93061.SAOUHSC_01838 STRING

⊟Protein sequence[edit | edit source]

  • MSDFNHTDHSTTNHSQTPRYRRPKFPWFKTVIVALIAGIIGALLVLGIGKVLNSTILNKDGSTVQTTNNKGGNQLDGQSKKFGTVHEMIKSVSPTIVGVINMQKASSVDDLLKGKSSKPSEAGVGSGVIYQINNNSAYIVTNNHVIDGANEIRVQLHNKKQVKAKLVGKDAVTDIAVLKIENTKGIKAIQFANSSKVQTGDSVFAMGNPLGLQFANSVTSGIISASERTIDAETTGGNTKVSVLQTDAAINPGNSGGALVDINGNLVGINSMKIAATQVEGIGFAIPSNEVKVTIEQLVKHGKIDRPSIGIGLINLKDIPEEEREQLHTDREDGIYVAKADSDIDLKKGDIITEIDGKKIKDDVDLRSYLYENKKPGESVTVTVIRDGKTKEVKVKLKQQKEQPKRQSRSERQSPGQGDRDFFR

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • ⊟interaction partners:
    SAOUHSC_01778(clpX)ATP-dependent protease ATP-binding subunit ClpX  [3] (data from MRSA252)
    SAOUHSC_01683(dnaK)molecular chaperone DnaK  [3] (data from MRSA252)
    SAOUHSC_00799(eno)phosphopyruvate hydratase  [3] (data from MRSA252)
    SAOUHSC_01246(infB)translation initiation factor IF-2  [3] (data from MRSA252)
    SAOUHSC_01424(murG)undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase  [3] (data from MRSA252)
    SAOUHSC_01753(obgE)GTPase ObgE  [3] (data from MRSA252)
    SAOUHSC_01235(pyrH)uridylate kinase  [3] (data from MRSA252)
    SAOUHSC_01262(recA)recombinase A  [3] (data from MRSA252)
    SAOUHSC_00519(rplA)50S ribosomal protein L1  [3] (data from MRSA252)
    SAOUHSC_02509(rplB)50S ribosomal protein L2  [3] (data from MRSA252)
    SAOUHSC_02512(rplC)50S ribosomal protein L3  [3] (data from MRSA252)
    SAOUHSC_02511(rplD)50S ribosomal protein L4  [3] (data from MRSA252)
    SAOUHSC_02500(rplE)50S ribosomal protein L5  [3] (data from MRSA252)
    SAOUHSC_02496(rplF)50S ribosomal protein L6  [3] (data from MRSA252)
    SAOUHSC_00520(rplJ)50S ribosomal protein L10  [3] (data from MRSA252)
    SAOUHSC_00518(rplK)50S ribosomal protein L11  [3] (data from MRSA252)
    SAOUHSC_00521(rplL)50S ribosomal protein L7/L12  [3] (data from MRSA252)
    SAOUHSC_02478(rplM)50S ribosomal protein L13  [3] (data from MRSA252)
    SAOUHSC_02502(rplN)50S ribosomal protein L14  [3] (data from MRSA252)
    SAOUHSC_02492(rplO)50S ribosomal protein L15  [3] (data from MRSA252)
    SAOUHSC_02505(rplP)50S ribosomal protein L16  [3] (data from MRSA252)
    SAOUHSC_02495(rplR)50S ribosomal protein L18  [3] (data from MRSA252)
    SAOUHSC_01211(rplS)50S ribosomal protein L19  [3] (data from MRSA252)
    SAOUHSC_01784(rplT)50S ribosomal protein L20  [3] (data from MRSA252)
    SAOUHSC_01757(rplU)50S ribosomal protein L21  [3] (data from MRSA252)
    SAOUHSC_02507(rplV)50S ribosomal protein L22  [3] (data from MRSA252)
    SAOUHSC_02510(rplW)50S ribosomal protein L23  [3] (data from MRSA252)
    SAOUHSC_00524(rpoB)DNA-directed RNA polymerase subunit beta  [3] (data from MRSA252)
    SAOUHSC_01829(rpsD)30S ribosomal protein S4  [3] (data from MRSA252)
    SAOUHSC_02494(rpsE)30S ribosomal protein S5  [3] (data from MRSA252)
    SAOUHSC_02477(rpsI)30S ribosomal protein S9  [3] (data from MRSA252)
    SAOUHSC_02503(rpsQ)30S ribosomal protein S17  [3] (data from MRSA252)
    SAOUHSC_00769(secA)preprotein translocase subunit SecA  [3] (data from MRSA252)
    SAOUHSC_02353(upp)uracil phosphoribosyltransferase  [3] (data from MRSA252)
    SAOUHSC_00153indolepyruvate decarboxylase  [3] (data from MRSA252)
    SAOUHSC_00187formate acetyltransferase  [3] (data from MRSA252)
    SAOUHSC_00222teichoic acid biosynthesis protein TagB  [3] (data from MRSA252)
    SAOUHSC_00467pur operon repressor  [3] (data from MRSA252)
    SAOUHSC_00472ribose-phosphate pyrophosphokinase  [3] (data from MRSA252)
    SAOUHSC_00525DNA-directed RNA polymerase subunit beta'  [3] (data from MRSA252)
    SAOUHSC_00529elongation factor G  [3] (data from MRSA252)
    SAOUHSC_00530elongation factor Tu  [3] (data from MRSA252)
    SAOUHSC_00535hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00742ribonucleotide-diphosphate reductase subunit alpha  [3] (data from MRSA252)
    SAOUHSC_00795glyceraldehyde-3-phosphate dehydrogenase  [3] (data from MRSA252)
    SAOUHSC_00875hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00878hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00947enoyl-(acyl carrier protein) reductase  [3] (data from MRSA252)
    SAOUHSC_01007bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [3] (data from MRSA252)
    SAOUHSC_01043dihydrolipoamide dehydrogenase  [3] (data from MRSA252)
    SAOUHSC_01150cell division protein FtsZ  [3] (data from MRSA252)
    SAOUHSC_01178bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase  [3] (data from MRSA252)
    SAOUHSC_01794glyceraldehyde 3-phosphate dehydrogenase 2  [3] (data from MRSA252)
    SAOUHSC_01801isocitrate dehydrogenase  [3] (data from MRSA252)
    SAOUHSC_01806pyruvate kinase  [3] (data from MRSA252)
    SAOUHSC_01814hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_01819hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_01820acetate kinase  [3] (data from MRSA252)
    SAOUHSC_01854hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_02107UDP-N-acetylmuramyl tripeptide synthetase  [3] (data from MRSA252)
    SAOUHSC_02301  [3] (data from MRSA252)
    SAOUHSC_02316DEAD-box ATP dependent DNA helicase  [3] (data from MRSA252)
    SAOUHSC_02377pyrimidine-nucleoside phosphorylase  [3] (data from MRSA252)
    SAOUHSC_02417  [3] (data from MRSA252)
    SAOUHSC_02441alkaline shock protein 23  [3] (data from MRSA252)
    SAOUHSC_0248630S ribosomal protein S11  [3] (data from MRSA252)
    SAOUHSC_02927malate:quinone oxidoreductase  [3] (data from MRSA252)
    SAOUHSC_02965carbamate kinase  [3] (data from MRSA252)
    SAOUHSC_02969arginine deiminase  [3] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

  • MicrobesOnline: no polycistronic organisation predicted

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

  • S.aureus Expression Data Browser:  [4] 
    Expression Data Browser
    ⊟Multi-gene expression profiles



    Click on any data point to display a description of the corresponding condition!

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

  • Aureolib: no data available

⊟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]

  1. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  2. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  3. ↑ Jump up to: 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 3.66 3.67 3.68 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)
  4. ↑ Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

⊟Relevant publications[edit | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SAOUHSC_01838&oldid=62645"
  • This page was last edited on 10 March 2016, at 16:33.
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