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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • pan locus tag?: SAUPAN003538000
  • symbol: sucD
  • pan gene symbol?: sucD
  • synonym:
  • product: succinyl-CoA synthetase subunit alpha

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • symbol: sucD
  • product: succinyl-CoA synthetase subunit alpha
  • replicon: chromosome
  • strand: +
  • coordinates: 1271840..1272748
  • length: 909
  • 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
    ATGAGTGTATTTATAGATAAGAATACTAAAGTAATGGTACAAGGTATTACAGGGTCTACT
    GCCCTTTTCCATACAAAACAAATGCTTGATTATGGTACGAAAATAGTAGCAGGTGTGACG
    CCTGGTAAAGGTGGTCAAGTTGTTGAAGGCGTTCCTGTTTTCAACACTGTTGAAGAAGCT
    AAAAATGAAACTGGGGCAACGGTTTCAGTCATTTACGTTCCAGCACCATTTGCTGCAGAC
    TCAATTTTAGAAGCAGCTGATGCAGACTTAGATATGGTTATTTGTATCACTGAACATATT
    CCTGTATTAGACATGGTTAAAGTTAAACGCTACTTACAAGGTAGAAAAACACGTTTAGTT
    GGTCCGAACTGTCCAGGTGTGATTACAGCAGATGAATGTAAAATTGGTATTATGCCTGGC
    TATATTCACAAAAAAGGTCATGTTGGTGTAGTATCTCGTTCAGGTACATTAACATATGAA
    GCAGTGCACCAATTGACTGAAGAAGGTATTGGTCAAACTACAGCTGTTGGTATTGGTGGA
    GACCCAGTCAACGGAACAAACTTTATTGATGTTTTAAAAGCATTCAATGAAGATGACGAA
    ACGAAAGCAGTTGTTATGATTGGTGAAATCGGTGGTACGGCTGAAGAAGAAGCAGCTGAA
    TGGATTAAAGCGAATATGACAAAACCAGTTGTAGGCTTTATCGGTGGACAAACAGCACCT
    CCTGGAAAACGTATGGGACATGCTGGTGCAATCATTTCAGGTGGTAAAGGTACTGCTGAA
    GAGAAAATTAAAACATTAAATAGTTGTGGTGTGAAAACAGCGGCAACACCTTCAGAAATT
    GGTTCAACATTAATTGAAGCTGCTAAAGAAGCAGGTATTTATGAATCATTATTAACTGTT
    AATAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    909

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • symbol: SucD
  • description: succinyl-CoA synthetase subunit alpha
  • length: 302
  • theoretical pI: 5.40845
  • theoretical MW: 31542
  • GRAVY: 0.0354305

⊟Function[edit | edit source]

  • ⊞⊞reaction:
    EC 6.2.1.5?  ExPASy
    Succinate--CoA ligase (ADP-forming) ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
  • ⊞⊞TIGRFAM:
    Metabolism Energy metabolism TCA cycle succinate-CoA ligase, alpha subunit (TIGR01019; EC 6.2.1.-; HMM-score: 479.4)
    and 1 more
    acetyl coenzyme A synthetase (ADP forming), alpha domain (TIGR02717; EC 6.2.1.13; HMM-score: 64.3)
  • ⊞⊞TheSEED  :
    • Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    and 2 more
    Carbohydrates Central carbohydrate metabolism TCA Cycle  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    Carbohydrates One-carbon Metabolism Serine-glyoxylate cycle  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
  • ⊞⊞PFAM:
    NADP_Rossmann (CL0063) CoA_binding; CoA binding domain (PF02629; HMM-score: 104.6)
    Succ_CoA_synth (CL0506) Ligase_CoA; CoA-ligase (PF00549; HMM-score: 91.2)
    and 2 more
    Succ_CoA_lig; Succinyl-CoA ligase like flavodoxin domain (PF13607; HMM-score: 37.7)
    NADP_Rossmann (CL0063) CoA_binding_2; CoA binding domain (PF13380; HMM-score: 25.3)

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

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

⊟Localization[edit | edit source]

  • ⊞⊞PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • ⊞⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.8794
    • Cytoplasmic Membrane Score: 0.0067
    • Cell wall & surface Score: 0.0003
    • Extracellular Score: 0.1136
  • ⊞⊞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): 0.018856
    • TAT(Tat/SPI): 0.002425
    • LIPO(Sec/SPII): 0.002333
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSVFIDKNTKVMVQGITGSTALFHTKQMLDYGTKIVAGVTPGKGGQVVEGVPVFNTVEEAKNETGATVSVIYVPAPFAADSILEAADADLDMVICITEHIPVLDMVKVKRYLQGRKTRLVGPNCPGVITADECKIGIMPGYIHKKGHVGVVSRSGTLTYEAVHQLTEEGIGQTTAVGIGGDPVNGTNFIDVLKAFNEDDETKAVVMIGEIGGTAEEEAAEWIKANMTKPVVGFIGGQTAPPGKRMGHAGAIISGGKGTAEEKIKTLNSCGVKTAATPSEIGSTLIEAAKEAGIYESLLTVNK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1012 [5]
  • ⊟⊟interaction partners:
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL2272(modA)molybdenum ABC transporter molybdenum-binding protein ModA  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL1696(ruvB)Holliday junction DNA helicase RuvB  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [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. ↑ Jump up to: 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 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]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1263&oldid=78157"
Insert paragraph

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • pan locus tag?: SAUPAN003538000
  • symbol: sucD
  • pan gene symbol?: sucD
  • synonym:
  • product: succinyl-CoA synthetase subunit alpha

Insert paragraph

⊟Genome View[edit | edit source]

Insert paragraph

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • symbol: sucD
  • product: succinyl-CoA synthetase subunit alpha
  • replicon: chromosome
  • strand: +
  • coordinates: 1271840..1272748
  • length: 909
  • essential: unknown other strains

Insert paragraph

⊟Accession numbers[edit | edit source]

Insert paragraph

⊟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
    ATGAGTGTATTTATAGATAAGAATACTAAAGTAATGGTACAAGGTATTACAGGGTCTACT
    GCCCTTTTCCATACAAAACAAATGCTTGATTATGGTACGAAAATAGTAGCAGGTGTGACG
    CCTGGTAAAGGTGGTCAAGTTGTTGAAGGCGTTCCTGTTTTCAACACTGTTGAAGAAGCT
    AAAAATGAAACTGGGGCAACGGTTTCAGTCATTTACGTTCCAGCACCATTTGCTGCAGAC
    TCAATTTTAGAAGCAGCTGATGCAGACTTAGATATGGTTATTTGTATCACTGAACATATT
    CCTGTATTAGACATGGTTAAAGTTAAACGCTACTTACAAGGTAGAAAAACACGTTTAGTT
    GGTCCGAACTGTCCAGGTGTGATTACAGCAGATGAATGTAAAATTGGTATTATGCCTGGC
    TATATTCACAAAAAAGGTCATGTTGGTGTAGTATCTCGTTCAGGTACATTAACATATGAA
    GCAGTGCACCAATTGACTGAAGAAGGTATTGGTCAAACTACAGCTGTTGGTATTGGTGGA
    GACCCAGTCAACGGAACAAACTTTATTGATGTTTTAAAAGCATTCAATGAAGATGACGAA
    ACGAAAGCAGTTGTTATGATTGGTGAAATCGGTGGTACGGCTGAAGAAGAAGCAGCTGAA
    TGGATTAAAGCGAATATGACAAAACCAGTTGTAGGCTTTATCGGTGGACAAACAGCACCT
    CCTGGAAAACGTATGGGACATGCTGGTGCAATCATTTCAGGTGGTAAAGGTACTGCTGAA
    GAGAAAATTAAAACATTAAATAGTTGTGGTGTGAAAACAGCGGCAACACCTTCAGAAATT
    GGTTCAACATTAATTGAAGCTGCTAAAGAAGCAGGTATTTATGAATCATTATTAACTGTT
    AATAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    909

Insert paragraph

This data comes from external databases and cannot be edited.

Insert paragraph

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1263 [new locus tag: SACOL_RS06450 ]
  • symbol: SucD
  • description: succinyl-CoA synthetase subunit alpha
  • length: 302
  • theoretical pI: 5.40845
  • theoretical MW: 31542
  • GRAVY: 0.0354305

Insert paragraph

⊟Function[edit | edit source]

  • ⊞reaction:
    EC 6.2.1.5?  ExPASy
    Succinate--CoA ligase (ADP-forming) ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
  • ⊞TIGRFAM:
    Metabolism Energy metabolism TCA cycle succinate-CoA ligase, alpha subunit (TIGR01019; EC 6.2.1.-; HMM-score: 479.4)
    and 1 more
    acetyl coenzyme A synthetase (ADP forming), alpha domain (TIGR02717; EC 6.2.1.13; HMM-score: 64.3)
  • ⊞TheSEED  :
    • Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    and 2 more
    Carbohydrates Central carbohydrate metabolism TCA Cycle  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
    Carbohydrates One-carbon Metabolism Serine-glyoxylate cycle  Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)
  • ⊞PFAM:
    NADP_Rossmann (CL0063) CoA_binding; CoA binding domain (PF02629; HMM-score: 104.6)
    Succ_CoA_synth (CL0506) Ligase_CoA; CoA-ligase (PF00549; HMM-score: 91.2)
    and 2 more
    Succ_CoA_lig; Succinyl-CoA ligase like flavodoxin domain (PF13607; HMM-score: 37.7)
    NADP_Rossmann (CL0063) CoA_binding_2; CoA binding domain (PF13380; HMM-score: 25.3)

Insert paragraph

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

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

Insert paragraph

⊟Localization[edit | edit source]

  • ⊞PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.8794
    • Cytoplasmic Membrane Score: 0.0067
    • Cell wall & surface Score: 0.0003
    • Extracellular Score: 0.1136
  • ⊞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): 0.018856
    • TAT(Tat/SPI): 0.002425
    • LIPO(Sec/SPII): 0.002333
  • predicted transmembrane helices (TMHMM): 0

Insert paragraph

⊟Accession numbers[edit | edit source]

Insert paragraph

⊟Protein sequence[edit | edit source]

  • MSVFIDKNTKVMVQGITGSTALFHTKQMLDYGTKIVAGVTPGKGGQVVEGVPVFNTVEEAKNETGATVSVIYVPAPFAADSILEAADADLDMVICITEHIPVLDMVKVKRYLQGRKTRLVGPNCPGVITADECKIGIMPGYIHKKGHVGVVSRSGTLTYEAVHQLTEEGIGQTTAVGIGGDPVNGTNFIDVLKAFNEDDETKAVVMIGEIGGTAEEEAAEWIKANMTKPVVGFIGGQTAPPGKRMGHAGAIISGGKGTAEEKIKTLNSCGVKTAATPSEIGSTLIEAAKEAGIYESLLTVNK

Insert paragraph

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1012 [5]
  • ⊟interaction partners:
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [6] (data from MRSA252)
    SACOL2272(modA)molybdenum ABC transporter molybdenum-binding protein ModA  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL1696(ruvB)Holliday junction DNA helicase RuvB  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

  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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 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)
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⊟Expression & Regulation[edit | edit source]

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⊟Operon[edit | edit source]

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⊟Regulation[edit | edit source]

  • regulator:

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