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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1448 [new locus tag: SACOL_RS07385 ]
  • pan locus tag?: SAUPAN003830000
  • symbol: sucB
  • pan gene symbol?: sucB
  • synonym:
  • product: dihydrolipoamide succinyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1448 [new locus tag: SACOL_RS07385 ]
  • symbol: sucB
  • product: dihydrolipoamide succinyltransferase
  • replicon: chromosome
  • strand: -
  • coordinates: 1459691..1460959
  • length: 1269
  • 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
    ATGCCAGAGGTTAAAGTTCCAGAATTAGCAGAATCTATTACAGAAGGTACCATTGCAGAA
    TGGTTGAAAAACGTAGGGGATAGCGTAGAAAAAGGTGAAGCTATTCTTGAATTAGAAACT
    GATAAAGTTAATGTCGAAGTTGTATCTGAAGAAGCAGGTGTATTATCTGAACAACTTGCA
    AGTGAAGGCGACACTGTAGAAGTTGGACAAGCAATTGCTATCATCGGCGAAGGTAGTGGC
    AATGCTTCTAAAGAAAATAGTAACGACAATACTCCACAACAAAATGAAGAAACAAATAAT
    AAAAAAGAAGAAACAACAAATAATTCGGTAGATAAAGCTGAAGTAAATCAAGCAAATGAT
    GACAATCAGCAACGTATTAATGCTACGCCTTCTGCGCGTCGATATGCTCGTGAAAATGGT
    GTGAATCTTGCTGAAGTAAGTCCGAAAACAAATGATGTGGTTCGTAAAGAAGATATTGAT
    AAGAAACAACAGGCACCGGCATCAACACAAACAACACAACAAGCATCTGCAAAAGAAGAG
    AAAAAATACAATCAATATCCTACAAAACCAGTGATTCGTGAAAAAATGTCACGTAGAAAG
    AAAACAGCTGCCAAAAAATTATTAGAGGTATCTAATAATACAGCTATGTTAACAACATTT
    AACGAAGTTGACATGACAAATGTTATGGAATTGCGTAAACGTAAGAAAGAACAATTTATG
    AAAGATCATGATGGTACTAAATTAGGATTTATGTCATTCTTTACTAAAGCTTCTGTAGCA
    GCTTTGAAAAAGTATCCAGAAGTTAATGCAGAAATCGACGGCGACGACATGATTACGAAA
    CAATATTATGATATTGGTGTAGCTGTTTCTACAGATGATGGATTATTAGTACCATTTGTA
    AGAGATTGTGATAAAAAGAATTTTGCAGAAATCGAAGCAGAAATTGCTAATTTAGCAGTT
    AAAGCACGAGAGAAAAAACTTGGCTTAGATGATATGGTTAATGGTTCATTTACGATTACA
    AATGGCGGTATTTTTGGATCAATGATGAGTACGCCAATTATCAATGGTAATCAAGCTGCA
    ATCTTAGGCATGCATTCAATTATTACAAGACCAATTGCGATTGATCAAGATACAATCGAA
    AATCGTCCAATGATGTATATTGCATTAAGCTATGATCATAGAATTATTGACGGTAAAGAA
    GCAGTTGGATTCTTAAAAACAATTAAAGAATTAATTGAAAACCCAGAAGACTTATTATTA
    GAATCTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1269

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1448 [new locus tag: SACOL_RS07385 ]
  • symbol: SucB
  • description: dihydrolipoamide succinyltransferase
  • length: 422
  • theoretical pI: 4.57447
  • theoretical MW: 46673.1
  • GRAVY: -0.611848

⊟Function[edit | edit source]

  • reaction:
    EC 2.3.1.61?  ExPASy
    Dihydrolipoyllysine-residue succinyltransferase Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
  • TIGRFAM:
    Metabolism Energy metabolism TCA cycle dihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 610.9)
    and 12 more
    2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase (TIGR02927; EC 2.3.1.61; HMM-score: 303.8)
    Metabolism Energy metabolism Pyruvate dehydrogenase dihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 269.1)
    Metabolism Energy metabolism Pyruvate dehydrogenase pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (TIGR01349; EC 2.3.1.12; HMM-score: 249.6)
    Metabolism Transport and binding proteins Cations and iron carrying compounds oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 22.6)
    Metabolism Energy metabolism Other oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 22.6)
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 21.4)
    Metabolism Transport and binding proteins Unknown substrate efflux transporter, RND family, MFP subunit (TIGR01730; HMM-score: 15.1)
    amphi-Trp domain (TIGR04354; HMM-score: 14.4)
    glycine cleavage protein H-like protein (TIGR03077; HMM-score: 10)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides 2'-Deoxyribonucleotide metabolism thymidylate synthase, flavin-dependent (TIGR02170; EC 2.1.1.148; HMM-score: 7.3)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 5.2)
    Metabolism Transport and binding proteins Cations and iron carrying compounds potassium uptake protein, Trk family (TIGR00934; HMM-score: 3.4)
  • TheSEED  :
    • Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61)
    Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes  Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61)
    and 2 more
    Carbohydrates Central carbohydrate metabolism TCA Cycle  Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61)
    Cofactors, Vitamins, Prosthetic Groups, Pigments Lipoic acid Lipoic acid metabolism  Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61)
  • PFAM:
    CoA-acyltrans (CL0149) 2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198; HMM-score: 266.8)
    and 9 more
    Hybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 76.6)
    no clan defined E3_binding; e3 binding domain (PF02817; HMM-score: 29.1)
    Hybrid (CL0105) Biotin_lipoyl_2; Biotin-lipoyl like (PF13533; HMM-score: 21.9)
    HlyD_3; HlyD family secretion protein (PF13437; HMM-score: 15.9)
    RnfC_N; RnfC Barrel sandwich hybrid domain (PF13375; HMM-score: 15.5)
    no clan defined IF3_N; Translation initiation factor IF-3, N-terminal domain (PF05198; HMM-score: 14.5)
    Hybrid (CL0105) PYNP_C; Pyrimidine nucleoside phosphorylase C-terminal domain (PF07831; HMM-score: 13.6)
    P-loop_NTPase (CL0023) LAP1C; Lamina-associated polypeptide 1C (LAP1C) (PF05609; HMM-score: 6.6)
    no clan defined DUF966; Domain of unknown function (DUF966) (PF06136; HMM-score: 6.6)

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

  • domains:
  • modifications:
  • cofactors: (R)-lipoate
  • 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): 0.003516
    • TAT(Tat/SPI): 0.000409
    • LIPO(Sec/SPII): 0.000396
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MPEVKVPELAESITEGTIAEWLKNVGDSVEKGEAILELETDKVNVEVVSEEAGVLSEQLASEGDTVEVGQAIAIIGEGSGNASKENSNDNTPQQNEETNNKKEETTNNSVDKAEVNQANDDNQQRINATPSARRYARENGVNLAEVSPKTNDVVRKEDIDKKQQAPASTQTTQQASAKEEKKYNQYPTKPVIREKMSRRKKTAAKKLLEVSNNTAMLTTFNEVDMTNVMELRKRKKEQFMKDHDGTKLGFMSFFTKASVAALKKYPEVNAEIDGDDMITKQYYDIGVAVSTDDGLLVPFVRDCDKKNFAEIEAEIANLAVKAREKKLGLDDMVNGSFTITNGGIFGSMMSTPIINGNQAAILGMHSIITRPIAIDQDTIENRPMMYIALSYDHRIIDGKEAVGFLKTIKELIENPEDLLLES

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 327 [5]
  • interaction partners:
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (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. ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  6. ↑ 6.0 6.1 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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