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PangenomeCOLN315NCTC8325NewmanUSA300_FPR375704-0298108BA0217611819-97685071193ECT-R 2ED133ED98HO 5096 0412JH1JH9JKD6008JKD6159LGA251M013MRSA252MSHR1132MSSA476MW2Mu3Mu50RF122ST398T0131TCH60TW20USA300_TCH1516VC40

NCBI: 06-JUL-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus Newman
  • locus tag: NWMN_0102 [new locus tag: NWMN_RS00570 ]
  • pan locus tag?: SAUPAN000982000
  • symbol: capH
  • pan gene symbol?: capH
  • synonym:
  • product: capsular polysaccharide synthesis enzyme O-acetyl transferase CapH

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: NWMN_0102 [new locus tag: NWMN_RS00570 ]
  • symbol: capH
  • product: capsular polysaccharide synthesis enzyme O-acetyl transferase CapH
  • replicon: chromosome
  • strand: +
  • coordinates: 126720..127346
  • length: 627
  • 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
    ATGAGGATAGCGATTGAAAAGATAATTGGTTTGCTGAAAAACCAGTCCTCTAAAGAATCG
    AATGTTAAGATTCATCGCTTGGCGTATATTACAAACTCAAAATTTGATGGCAATAACTAT
    ATAGATAGATGGTGTAAAATCAGGAATTCTCACATTGGTGAATACAGTTATATTGGATTT
    GGTAGTGATTTTAATAATGTAGAAGTAGGAAGATATTGTTCGATATCTTCGGATGTAAAA
    ATTGGGTTAGGAAAACATCCTACACACTTTTTTAGCTCATCACCGATTTTTTATTCTAAT
    AATAATCCATTTAACATAAAGCAAAAGTTTATAGACTTTAATGACCAACCAAGCCGTACA
    ACAATTAAAAATGATGTGTGGATTGGTGCAAATGTAATTATTATGGATGGTTTAACAATA
    AATACTGGTGCAGTCATAGCAGCCGGCTCAGTTGTTACTAAAAATGTAGGAGCATATGAG
    GTTGTTGGTGGTGTTCCTGCAAAAGTGATTAAGAAGCGATTTGACAATAAAACAATTGAA
    AAACTTTTGGAAAGCAAGTGGTGGGAGAAAACGCCTGACAAACTAAAAGGATTTTCGGTT
    GAATATTTAAATAAAAAGGATACTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    627

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: NWMN_0102 [new locus tag: NWMN_RS00570 ]
  • symbol: CapH
  • description: capsular polysaccharide synthesis enzyme O-acetyl transferase CapH
  • length: 208
  • theoretical pI: 10.0346
  • theoretical MW: 23476.7
  • GRAVY: -0.373558

⊟Function[edit | edit source]

  • TIGRFAM:
    phosphonate metabolim protein, transferase hexapeptide repeat family (TIGR03308; HMM-score: 134.3)
    and 13 more
    2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase (TIGR03532; EC 2.3.1.89; HMM-score: 62.7)
    sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family (TIGR03570; HMM-score: 43.7)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 37.8)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 37.8)
    Metabolism Central intermediary metabolism Amino sugars UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 37.8)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD (TIGR01853; EC 2.3.1.191; HMM-score: 32.5)
    glucose-1-phosphate thymidylyltransferase (TIGR01208; EC 2.7.7.24; HMM-score: 31.6)
    Metabolism Amino acid biosynthesis Serine family serine O-acetyltransferase (TIGR01172; EC 2.3.1.30; HMM-score: 30.4)
    colanic acid biosynthesis acetyltransferase WcaF (TIGR04008; EC 2.3.1.-; HMM-score: 29.4)
    Metabolism Energy metabolism Other phenylacetic acid degradation protein PaaY (TIGR02287; HMM-score: 22.7)
    colanic acid biosynthesis acetyltransferase WcaB (TIGR04016; EC 2.3.1.-; HMM-score: 22.3)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (TIGR01852; EC 2.3.1.129; HMM-score: 18)
    UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03992; EC 2.3.1.157,2.7.7.23; HMM-score: 11)
  • TheSEED: data available for COL, N315, NCTC8325, USA300_FPR3757
  • PFAM:
    HEXAPEP (CL0536) Hexapep; Bacterial transferase hexapeptide (six repeats) (PF00132; HMM-score: 50.1)
    and 2 more
    Hexapep_2; Hexapeptide repeat of succinyl-transferase (PF14602; HMM-score: 25)
    no clan defined DUF411; Protein of unknown function, DUF (PF04214; HMM-score: 12.6)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.055498
    • TAT(Tat/SPI): 0.000935
    • LIPO(Sec/SPII): 0.002957
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MRIAIEKIIGLLKNQSSKESNVKIHRLAYITNSKFDGNNYIDRWCKIRNSHIGEYSYIGFGSDFNNVEVGRYCSISSDVKIGLGKHPTHFFSSSPIFYSNNNPFNIKQKFIDFNDQPSRTTIKNDVWIGANVIIMDGLTINTGAVIAAGSVVTKNVGAYEVVGGVPAKVIKKRFDNKTIEKLLESKWWEKTPDKLKGFSVEYLNKKDT

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulators: CodY (repression) regulon, SigB (activation) regulon
    CodY(TF)important in Amino acid metabolism; RegPrecise    transcription unit transferred from N315 data RegPrecise 
    SigB(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation;  [3] [4]   other strains

⊟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. ↑ Daniela Keinhörster, Shilpa Elizabeth George, Christopher Weidenmaier, Christiane Wolz
    Function and regulation of Staphylococcus aureus wall teichoic acids and capsular polysaccharides.
    Int J Med Microbiol: 2019, 309(6);151333
    [PubMed:31362856] [WorldCat.org] [DOI] (I p)
  2. ↑ S Sau, J Sun, C Y Lee
    Molecular characterization and transcriptional analysis of type 8 capsule genes in Staphylococcus aureus.
    J Bacteriol: 1997, 179(5);1614-21
    [PubMed:9045821] [WorldCat.org] [DOI] (P p)
  3. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  4. ↑ Bettina Schulthess, Dominik A Bloes, Patrice François, Myriam Girard, Jacques Schrenzel, Markus Bischoff, Brigitte Berger-Bächi
    The σB-dependent yabJ-spoVG operon is involved in the regulation of extracellular nuclease, lipase, and protease expression in Staphylococcus aureus.
    J Bacteriol: 2011, 193(18);4954-62
    [PubMed:21725011] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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