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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • pan locus tag?: SAUPAN004387000
  • symbol: SACOL1777
  • pan gene symbol?: htrA1
  • synonym:
  • product: serine protease HtrA

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • symbol: SACOL1777
  • product: serine protease HtrA
  • replicon: chromosome
  • strand: +
  • coordinates: 1817258..1818532
  • length: 1275
  • 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
    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: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • symbol: SACOL1777
  • description: serine protease HtrA
  • 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, DegP/HtrA, do-like (EC 3.4.21.-)
  • ⊞⊞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]

⊟Protein sequence[edit | edit source]

  • MSDFNHTDHSTTNHSQTPRYRRPKFPWFKTVIVALIAGIIGALLVLGIGKVLNSTILNKDGSTVQTTNNKGGNQLDGQSKKFGTVHEMIKSVSPTIVGVINMQKASSVDDLLKGKSSKPSEAGVGSGVIYQINNNSAYIVTNNHVIDGANEIRVQLHNKKQVKAKLVGKDAVTDIAVLKIENTKGIKAIQFANSSKVQTGDSVFAMGNPLGLQFANSVTSGIISASERTIDAETTGGNTKVSVLQTDAAINPGNSGGALVDINGNLVGINSMKIAATQVEGIGFAIPSNEVKVTIEQLVKHGKIDRPSIGIGLINLKDIPEEEREQLHTDREDGIYVAKADSDIDLKKGDIITEIDGKKIKDDVDLRSYLYENKKPGESVTVTVIRDGKTKEVKVKLKQQKEQPKRQSRSERQSPGQGDRDFFR

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Integral membrane [1] [2] [3] [4]
  • quantitative data / protein copy number per cell:
  • ⊟⊟interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL2654(arcC2)carbamate kinase  [5] (data from MRSA252)
    SACOL1721(clpX)ATP-dependent protease ATP-binding subunit ClpX  [5] (data from MRSA252)
    SACOL1223(coaBC)phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [5] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [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)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SACOL0173(ipdC)indole-3-pyruvate decarboxylase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL1453(murG)UDPdiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase  [5] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [5] (data from MRSA252)
    SACOL1699(obgE)GTPase ObgE  [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)
    SACOL0544(prsA)ribose-phosphate pyrophosphokinase  [5] (data from MRSA252)
    SACOL0539(purR)pur operon repressor  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL1277(pyrH)uridylate kinase  [5] (data from MRSA252)
    SACOL1304(recA)recombinase A  [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)
    SACOL2229(rplN)50S ribosomal protein L14  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [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)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL2057(rsbU)sigma factor B regulator protein  [5] (data from MRSA252)
    SACOL0816(secA)preprotein translocase subunit SecA  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL0238teichoic acid biosynthesis protein  [5] (data from MRSA252)
    SACOL0599hypothetical protein  [5] (data from MRSA252)
    SACOL0941  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL1788hypothetical protein  [5] (data from MRSA252)
    SACOL1951Mur ligase  [5] (data from MRSA252)
    SACOL2072DEAD/DEAH box helicase  [5] (data from MRSA252)
    SACOL2156ATP-binding Mrp/Nbp35 family protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (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: 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. ↑ 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. ↑ Jump up to: 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 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)

⊟Relevant publications[edit | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1777&oldid=81475"
Insert paragraph

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • pan locus tag?: SAUPAN004387000
  • symbol: SACOL1777
  • pan gene symbol?: htrA1
  • synonym:
  • product: serine protease HtrA

Insert paragraph

⊟Genome View[edit | edit source]

Insert paragraph

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • symbol: SACOL1777
  • product: serine protease HtrA
  • replicon: chromosome
  • strand: +
  • coordinates: 1817258..1818532
  • length: 1275
  • essential: unknown other strains

Insert paragraph

⊟Accession numbers[edit | edit source]

Insert paragraph

⊟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

Insert paragraph

This data comes from external databases and cannot be edited.

Insert paragraph

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1777 [new locus tag: SACOL_RS09095 ]
  • symbol: SACOL1777
  • description: serine protease HtrA
  • length: 424
  • theoretical pI: 9.97226
  • theoretical MW: 45802.6
  • GRAVY: -0.416981

Insert paragraph

⊟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, DegP/HtrA, do-like (EC 3.4.21.-)
  • ⊞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)

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

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

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⊟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

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⊟Accession numbers[edit | edit source]

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⊟Protein sequence[edit | edit source]

  • MSDFNHTDHSTTNHSQTPRYRRPKFPWFKTVIVALIAGIIGALLVLGIGKVLNSTILNKDGSTVQTTNNKGGNQLDGQSKKFGTVHEMIKSVSPTIVGVINMQKASSVDDLLKGKSSKPSEAGVGSGVIYQINNNSAYIVTNNHVIDGANEIRVQLHNKKQVKAKLVGKDAVTDIAVLKIENTKGIKAIQFANSSKVQTGDSVFAMGNPLGLQFANSVTSGIISASERTIDAETTGGNTKVSVLQTDAAINPGNSGGALVDINGNLVGINSMKIAATQVEGIGFAIPSNEVKVTIEQLVKHGKIDRPSIGIGLINLKDIPEEEREQLHTDREDGIYVAKADSDIDLKKGDIITEIDGKKIKDDVDLRSYLYENKKPGESVTVTVIRDGKTKEVKVKLKQQKEQPKRQSRSERQSPGQGDRDFFR

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⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Integral membrane [1] [2] [3] [4]
  • quantitative data / protein copy number per cell:
  • ⊟interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL2654(arcC2)carbamate kinase  [5] (data from MRSA252)
    SACOL1721(clpX)ATP-dependent protease ATP-binding subunit ClpX  [5] (data from MRSA252)
    SACOL1223(coaBC)phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [5] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [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)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SACOL0173(ipdC)indole-3-pyruvate decarboxylase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL1453(murG)UDPdiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase  [5] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [5] (data from MRSA252)
    SACOL1699(obgE)GTPase ObgE  [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)
    SACOL0544(prsA)ribose-phosphate pyrophosphokinase  [5] (data from MRSA252)
    SACOL0539(purR)pur operon repressor  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL1277(pyrH)uridylate kinase  [5] (data from MRSA252)
    SACOL1304(recA)recombinase A  [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)
    SACOL2229(rplN)50S ribosomal protein L14  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [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)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [5] (data from MRSA252)
    SACOL2057(rsbU)sigma factor B regulator protein  [5] (data from MRSA252)
    SACOL0816(secA)preprotein translocase subunit SecA  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL0238teichoic acid biosynthesis protein  [5] (data from MRSA252)
    SACOL0599hypothetical protein  [5] (data from MRSA252)
    SACOL0941  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL1753universal stress protein  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL1788hypothetical protein  [5] (data from MRSA252)
    SACOL1951Mur ligase  [5] (data from MRSA252)
    SACOL2072DEAD/DEAH box helicase  [5] (data from MRSA252)
    SACOL2156ATP-binding Mrp/Nbp35 family protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)

  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. ↑ 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 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)
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⊟Expression & Regulation[edit | edit source]

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⊟Operon[edit | edit source]

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⊟Regulation[edit | edit source]

  • regulator:

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⊟Transcription pattern[edit | edit source]

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

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⊟Protein stability[edit | edit source]

  • half-life: no data available

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⊞Biological Material[edit | edit source]

This data comes from external databases and cannot be edited.

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⊞Other Information[edit | edit source]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

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⊟Relevant publications[edit | edit source]

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