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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0699 [new locus tag: SACOL_RS03595 ]
  • pan locus tag?: SAUPAN002519000
  • symbol: pbp4
  • pan gene symbol?: pbp4
  • synonym:
  • product: penicillin-binding protein 4

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0699 [new locus tag: SACOL_RS03595 ]
  • symbol: pbp4
  • product: penicillin-binding protein 4
  • replicon: chromosome
  • strand: -
  • coordinates: 722930..724225
  • length: 1296
  • 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
    ATGAAAAATTTAATATCTATTATCATCATTTTATGTTTAACATTAAGTATTATGACACCA
    TATGCACAAGCTACTAACAGTGACGTAACCCCTGTACAAGCAGCAAATCAATATGGTTAT
    GCAGGTTTGTCGGCTGCATACGAACCGACGAGTGCTGTTAATGTAAGTCAAACTGGACAA
    TTACTGTATCAATACAATATCGATACTAAGTGGAATCCAGCGTCTATGACTAAATTAATG
    ACAATGTACTTAACATTGGAAGCTGTAAATAAGGGGCAGCTTTCACTTGATGACACAGTC
    ACAATGACGAACAAAGAATATATTATGTCTACACTACCTGAGTTGAGTAATACGAAACTA
    TATCCTGGACAAGTATGGACAATCGCAGACCTATTACAAATTACAGTATCTAATTCTAGT
    AATGCCGCGGCATTAATTTTAGCTAAGAAGGTTTCAAAAAACACCAGCGATTTCGTTGAT
    TTAATGAATAACAAAGCTAAAGCTATCGGAATGAAAAATACACATTTCGTCAATCCAACG
    GGTGCTGAAAATTCAAGATTACGTACATTTGCACCAACAAAGTATAAAGACCAAGAACGT
    ACTGTAACGACTGCTAGAGACTATGCCATTTTAGATTTACACGTGATTAAAGAGACACCT
    AAAATATTAGACTTTACAAAGCAGTTAGCACCAACAACGCATGCAGTTACGTATTACACA
    TTCAACTTTTCATTGGAAGGTGCAAAAATGAGTTTGCCGGGTACAGATGGTTTAAAAACT
    GGATCAAGTGATACAGCAAATTACAACCATACGATTACTACCAAACGAGGTAAATTTAGA
    ATTAATCAAGTTATCATGGGTGCAGGAGACTATAAAAACCTTGGTGGCGAGAAGCAACGT
    AATATGATGGGGAATGCATTAATGGAACGCTCATTTGATCAGTATAAATATGTAAAAATA
    TTGTCTAAAGGTGAGCAAAGGATAAATGGTAAGAAATATTATGTTGAAAATGATCTTTAC
    GATGTTTTACCAAGTGATTTTAGTAAAAAAGATTATAAACTTGTAGTCGAAGATGGTAAA
    GTACACGCGGACTATCCAAGAGAATTTATTAATAAAGATTATGGACCTCCAACTGTAGAA
    GTTCATCAGCCAATTATTCAAAAGGCAAATACTGTTGCTAAAAGTATGTGGGAAGAACAT
    CCATTATTCACTATCATTGGTGGTACATGCCTTGTCGCTGGATTAGCACTTATTGTTCAT
    ATGATAATCAATCGTTTATTTAGAAAAAGAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1296

⊟Protein[edit | edit source]

Protein Data Bank: 3HUM
Protein Data Bank: 3HUN

⊟General[edit | edit source]

  • locus tag: SACOL0699 [new locus tag: SACOL_RS03595 ]
  • symbol: Pbp4
  • description: penicillin-binding protein 4
  • length: 431
  • theoretical pI: 9.63301
  • theoretical MW: 48261.2
  • GRAVY: -0.310905

⊟Function[edit | edit source]

  • TIGRFAM:
  • TheSEED  :
    • D-alanyl-D-alanine carboxypeptidase (EC 3.4.16.4)
    • Penicillin binding protein PBP4
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory Murein Hydrolases  D-alanyl-D-alanine carboxypeptidase (EC 3.4.16.4)
    and 1 more
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory Peptidoglycan Biosynthesis  D-alanyl-D-alanine carboxypeptidase (EC 3.4.16.4)
  • PFAM:
    Beta-lactamase (CL0013) Peptidase_S11; D-alanyl-D-alanine carboxypeptidase (PF00768; HMM-score: 176.1)
    and 4 more
    no clan defined DUF1958; Domain of unknown function (DUF1958) (PF09211; HMM-score: 104)
    Beta-lactamase (CL0013) Beta-lactamase2; Beta-lactamase enzyme family (PF13354; HMM-score: 63.9)
    Beta-lactamase; Beta-lactamase (PF00144; HMM-score: 38.4)
    Peptidase_S13; D-Ala-D-Ala carboxypeptidase 3 (S13) family (PF02113; HMM-score: 14.1)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 0
    • Cytoplasmic Membrane Score: 9.68
    • Cellwall Score: 0.17
    • Extracellular Score: 0.16
    • Internal Helices: 2
  • LocateP: Multi-transmembrane
    • Prediction by SwissProt Classification: Membrane
    • Pathway Prediction: Sec-(SPI)
    • Intracellular possibility: 0
    • Signal peptide possibility: 1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: Signal peptide SP(Sec/SPI) length 24 aa
    • SP(Sec/SPI): 0.997708
    • TAT(Tat/SPI): 0.000514
    • LIPO(Sec/SPII): 0.001243
    • Cleavage Site: CS pos: 24-25. AQA-TN. Pr: 0.9185
  • predicted transmembrane helices (TMHMM): 1

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKNLISIIIILCLTLSIMTPYAQATNSDVTPVQAANQYGYAGLSAAYEPTSAVNVSQTGQLLYQYNIDTKWNPASMTKLMTMYLTLEAVNKGQLSLDDTVTMTNKEYIMSTLPELSNTKLYPGQVWTIADLLQITVSNSSNAAALILAKKVSKNTSDFVDLMNNKAKAIGMKNTHFVNPTGAENSRLRTFAPTKYKDQERTVTTARDYAILDLHVIKETPKILDFTKQLAPTTHAVTYYTFNFSLEGAKMSLPGTDGLKTGSSDTANYNHTITTKRGKFRINQVIMGAGDYKNLGGEKQRNMMGNALMERSFDQYKYVKILSKGEQRINGKKYYVENDLYDVLPSDFSKKDYKLVVEDGKVHADYPREFINKDYGPPTVEVHQPIIQKANTVAKSMWEEHPLFTIIGGTCLVAGLALIVHMIINRLFRKRK

⊟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:
    SACOL1494(asnC)asparaginyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [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)
    SACOL1091(ptsH)phosphocarrier protein HPr  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [5] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [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)
    SACOL1238(rpmB)50S ribosomal protein L28  [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)
    SACOL0591(rpsL)30S ribosomal protein S12  [5] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SACOL0439(rpsR)30S ribosomal protein S18  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL0506ABC transporter substrate-binding protein  [5] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [5] (data from MRSA252)
    SACOL2163hypothetical protein  [5] (data from MRSA252)
    SACOL2561hydroxymethylglutaryl-CoA synthase  [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. ↑ 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 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]

Vikas Navratna, Savitha Nadig, Varun Sood, K Prasad, Gayathri Arakere, B Gopal
Molecular basis for the role of Staphylococcus aureus penicillin binding protein 4 in antimicrobial resistance.
J Bacteriol: 2010, 192(1);134-44
[PubMed:19854906] [WorldCat.org] [DOI] (I p)

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