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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS12645 [old locus tag: SA2204 ]
  • pan locus tag?: SAUPAN005952000
  • symbol: SA_RS12645
  • pan gene symbol?: gpmA
  • synonym:
  • product: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA_RS12645 [old locus tag: SA2204 ]
  • symbol: SA_RS12645
  • product: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
  • replicon: chromosome
  • strand: -
  • coordinates: 2473572..2474258
  • length: 687
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (2473572..2474258) NCBI
  • BioCyc: SA_RS12645 BioCyc
  • MicrobesOnline: see SA2204

⊟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
    ATGCCAAAATTAATTTTATGTCGTCATGGACAAAGCGAGTGGAATGCTAAAAACTTATTT
    ACTGGATGGGAAGATGTTAATTTATCTGAACAAGGTATTAATGAAGCGACTAGAGCAGGT
    GAAAAAGTAAGAGAAAATAACATTGCCATCGATGTAGCTTTTACATCGTTATTAACACGT
    GCTTTAGATACAACGCATTATATTTTAACTGAATCTAAACAACAATGGATTCCTGTATAT
    AAAAGCTGGCGTTTAAATGAACGCCACTATGGTGGATTGCAAGGCTTAAATAAAGATGAT
    GCTAGAAAAGAATTTGGAGAAGAACAAGTACATATTTGGCGTCGTTCTTATGATGTGAAA
    CCACCTGCTGAAACCGAAGAACAACGTGAAGCTTACTTAGCTGATCGTCGATATAATCAT
    TTAGATAAACGTATGATGCCTTATTCTGAAAGTCTGAAAGATACTTTAGTTCGAGTGATA
    CCATTTTGGACAGATCATATTTCACAATATTTGCTAGATGGTCAAACGGTATTAGTTTCT
    GCACACGGAAATTCAATTCGCGCATTAATTAAATATCTTGAAGATGTGTCAGATGAAGAT
    ATCATTAATTATGAAATTAAAACAGGTGCACCGCTTGTTTATGAATTAACGGATGATTTA
    GAAGTTATAGATAAATACTACTTATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    687

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA_RS12645 [old locus tag: SA2204 ]
  • symbol: SA_RS12645
  • description: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
  • length: 228
  • theoretical pI: 5.05486
  • theoretical MW: 26679.8
  • GRAVY: -0.632018

⊟Function[edit | edit source]

  • reaction:
    EC 5.4.2.11?  ExPASy
    Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) 2-phospho-D-glycerate = 3-phospho-D-glycerate
  • TIGRFAM:
    phosphoglycerate mutase 1 family (TIGR01258; HMM-score: 332.9)
    and 3 more
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin alpha-ribazole phosphatase (TIGR03162; EC 3.1.3.73; HMM-score: 79.1)
    probable phosphomutase, MSMEG_4193 family (TIGR03848; EC 5.4.2.-; HMM-score: 39.2)
    Signal transduction Regulatory functions Protein interactions phosphohistidine phosphatase SixA (TIGR00249; EC 3.1.3.-; HMM-score: 22.7)
  • TheSEED: see SA2204
  • PFAM:
    His_phosphatase (CL0071) His_Phos_1; Histidine phosphatase superfamily (branch 1) (PF00300; HMM-score: 127.6)

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

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

⊟Localization[edit | edit source]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • Internal Helices: 0
  • LocateP:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.006454
    • TAT(Tat/SPI): 0.000508
    • LIPO(Sec/SPII): 0.001283
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVYKSWRLNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETEEQREAYLADRRYNHLDKRMMPYSESLKDTLVRVIPFWTDHISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDIINYEIKTGAPLVYELTDDLEVIDKYYL

⊟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: data available for COL
  • interaction partners:
    SA_RS00690immunoglobulin G-binding protein A  [1] (data from MRSA252)
    SA_RS01275formate acetyltransferase  [1] (data from MRSA252)
    SA_RS0201530S ribosomal protein S6  [1] (data from MRSA252)
    SA_RS0291550S ribosomal protein L10  [1] (data from MRSA252)
    SA_RS0294530S ribosomal protein S12  [1] (data from MRSA252)
    SA_RS02955elongation factor G  [1] (data from MRSA252)
    SA_RS02960elongation factor Tu  [1] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [1] (data from MRSA252)
    SA_RS04895NAD(+) kinase  [1] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA_RS05355pyruvate dehydrogenase E1 component subunit beta  [1] (data from MRSA252)
    SA_RS05360dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  [1] (data from MRSA252)
    SA_RS05365dihydrolipoyl dehydrogenase  [1] (data from MRSA252)
    SA_RS0614050S ribosomal protein L19  [1] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [1] (data from MRSA252)
    SA_RS07060dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex  [1] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [1] (data from MRSA252)
    SA_RS07955molecular chaperone DnaK  [1] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [1] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [1] (data from MRSA252)
    SA_RS08560pyruvate kinase  [1] (data from MRSA252)
    SA_RS08625universal stress protein UspA  [1] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [1] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [1] (data from MRSA252)
    SA_RS1173050S ribosomal protein L16  [1] (data from MRSA252)
    SA_RS1173530S ribosomal protein S3  [1] (data from MRSA252)
    SA_RS13920arginine deiminase  [1] (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. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 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]

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