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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

General[edit source | edit]

  • 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 source | edit]

  • reaction:
    EC 2.3.1.61?  ExPASy
    Dihydrolipoyllysine-residue succinyltransferaseSuccinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
  • TIGRFAM:
    MetabolismEnergy metabolismTCA cycledihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 610.9)
    2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase (TIGR02927; EC 2.3.1.61; HMM-score: 303.8)
    MetabolismEnergy metabolismPyruvate dehydrogenasedihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 269.1)
    MetabolismEnergy metabolismPyruvate dehydrogenasepyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (TIGR01349; EC 2.3.1.12; HMM-score: 249.6)
    MetabolismTransport and binding proteinsCations and iron carrying compoundsoxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 22.6)
    MetabolismEnergy metabolismOtheroxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 22.6)
    MetabolismCentral intermediary metabolismNitrogen metabolismurea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 21.4)
    MetabolismTransport and binding proteinsUnknown substrateefflux 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)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotides2'-Deoxyribonucleotide metabolismthymidylate synthase, flavin-dependent (TIGR02170; EC 2.1.1.148; HMM-score: 7.3)
    MetabolismFatty acid and phospholipid metabolismBiosynthesisacetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 5.2)
    MetabolismTransport and binding proteinsCations and iron carrying compoundspotassium uptake protein, Trk family (TIGR00934; HMM-score: 3.4)
  • TheSEED:  
    CarbohydratesCentral carbohydrate metabolismDehydrogenase complexes Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) 
    Central carbohydrate metabolismTCA Cycle Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) 
    Cofactors, Vitamins, Prosthetic Groups, PigmentsLipoic acidLipoic 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)
    Hybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 76.6)
    no clan definedE3_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 definedIF3_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 definedDUF966; Domain of unknown function (DUF966) (PF06136; HMM-score: 6.6)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors: (R)-lipoate
  • effectors:
  • protein partners:
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [1] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.1
    • Ymax_pos: 31
    • Cmax: 0.11
    • Cmax_pos: 28
    • Smax: 0.119
    • Smax_pos: 27
    • Smean: 0.078
    • D: 0.091
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MPEVKVPELAESITEGTIAEWLKNVGDSVEKGEAILELETDKVNVEVVSEEAGVLSEQLASEGDTVEVGQAIAIIGEGSGNASKENSNDNTPQQNEETNNKKEETTNNSVDKAEVNQANDDNQQRINATPSARRYARENGVNLAEVSPKTNDVVRKEDIDKKQQAPASTQTTQQASAKEEKKYNQYPTKPVIREKMSRRKKTAAKKLLEVSNNTAMLTTFNEVDMTNVMELRKRKKEQFMKDHDGTKLGFMSFFTKASVAALKKYPEVNAEIDGDDMITKQYYDIGVAVSTDDGLLVPFVRDCDKKNFAEIEAEIANLAVKAREKKLGLDDMVNGSFTITNGGIFGSMMSTPIINGNQAAILGMHSIITRPIAIDQDTIENRPMMYIALSYDHRIIDGKEAVGFLKTIKELIENPEDLLLES

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5]
    quantitative data / protein copy number per cell: 327 [6]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. 1.0 1.1 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)
  2. 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)
  3. 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)
  4. 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)
  5. 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)
  6. 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)

Relevant publications[edit source | edit]