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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1560 [new locus tag: SACOL_RS07945 ]
- pan locus tag?: SAUPAN004070000
- symbol: SACOL1560
- pan gene symbol?: bfmBB
- synonym: bkdB
- product: 2-oxoisovalerate dehydrogenase, E2 component, dihydrolipoamide acetyltransferase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1560 [new locus tag: SACOL_RS07945 ]
- symbol: SACOL1560
- product: 2-oxoisovalerate dehydrogenase, E2 component, dihydrolipoamide acetyltransferase
- replicon: chromosome
- strand: -
- coordinates: 1595256..1596530
- length: 1275
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237932 NCBI
- RefSeq: YP_186401 NCBI
- BioCyc: see SACOL_RS07945
- MicrobesOnline: 913009 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1261ATGGAAATAACAATGCCTAAGTTAGGTGAGAGTGTTCATGAAGGCACCATTGAACAATGG
TTAGTTTCTGTTGGTGATCATATTGATGAATATGAACCATTATGTGAAGTTATTACAGAT
AAAGTGACAGCTGAAGTCCCTTCCACGATATCAGGAACAATTACAGAAATTTTAGTTGAA
GCGGGGCAGACAGTAGCTATTGATACAATTATCTGTAAAATTGAAACTGCTGATGAAAAG
ACAAATGAAACAACTGAAGAGATACAAGCAAAAGTGGATGAGCATACTCAGAAATCTACT
AAAAAAGCTAGTGCAACAGTGGAACAGACATCTACTGCTAAACAAAATCAACCACGTAAT
AATGGTCGCTTTTCACCTGTTGTATTTAAACTCGCTTCAGAGCATGACATTGATTTATCA
CAAGTTGTAGGTAGTGGATTTGAAGGTCGTGTAACTAAGAAGGATATAATGTCAGTTATT
GAAAATGGTGGTACCACAGCTCAATCTGACAAACAAGTTCAAACAAAATCAACATCAGTA
GATACATCAAGTAACCAATCATCTGAAGACAATAGTGAAAACAGCACAATACCAGTAAAT
GGTGTGCGTAAAGCAATTGCGCAAAATATGGTTAATAGTGTAACAGAGATTCCACATGCA
TGGATGATGATTGAAGTAGATGCTACAAATCTTGTGAAAACGAGAAATCATTATAAAAAC
AGCTTTAAAAATAAAGAAGGATATAATCTAACGTTCTTTGCTTTCTTTGTAAAAGCTGTA
GCAGATGCTTTAAAAGCATATCCTTTATTAAATAGTAGCTGGCAAGGAAATGAAATTGTC
TTACATAAAGACATTAATATTTCAATTGCTGTTGCTGATGAAAATAAATTATACGTACCT
GTGATTAAGCATGCAGACGAAAAGTCAATCAAAGGTATAGCTAGAGAAATTAATACTTTA
GCAACGAAAGCGCGTAATAAGCAATTGACAGCTGAAGATATGCAGGGCGGTACATTTACG
GTAAATAATACTGGTACATTTGGTTCAGTATCATCAATGGGTATTATAAATCATCCACAA
GCAGCGATTTTACAAGTAGAATCAATCGTTAAAAAGCCAGTAGTAATTAATGATATGATT
GCAATTCGTAACATGGTTAATTTATGTATTTCAATTGATCATCGTATTTTAGATGGTTTA
CAAACAGGTAAATTTATGAATCATATTAAACAGCGTATCGAACAGTATACTTTAGAAAAT
ACAAATATATATTAG60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1560 [new locus tag: SACOL_RS07945 ]
- symbol: SACOL1560
- description: 2-oxoisovalerate dehydrogenase, E2 component, dihydrolipoamide acetyltransferase
- length: 424
- theoretical pI: 5.46533
- theoretical MW: 46739.5
- GRAVY: -0.34033
⊟Function[edit | edit source]
- reaction: EC 2.3.1.-? ExPASy
- TIGRFAM: 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase (TIGR02927; EC 2.3.1.61; HMM-score: 332.8)Energy metabolism TCA cycle dihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 316.3)Energy metabolism Pyruvate dehydrogenase pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (TIGR01349; EC 2.3.1.12; HMM-score: 277.8)and 4 moreEnergy metabolism Pyruvate dehydrogenase dihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 252.5)Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 19.1)Transport and binding proteins Cations and iron carrying compounds oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 14.6)Energy metabolism Other oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 14.6)
- TheSEED :
- Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168)
Amino Acids and Derivatives Branched-chain amino acids Isoleucine degradation Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168)and 3 moreAmino Acids and Derivatives Branched-chain amino acids Valine degradation Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168) - PFAM: CoA-acyltrans (CL0149) 2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198; HMM-score: 272)and 7 moreHybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 80.3)no clan defined E3_binding; e3 binding domain (PF02817; HMM-score: 42.2)Hybrid (CL0105) Biotin_lipoyl_2; Biotin-lipoyl like (PF13533; HMM-score: 22.4)HlyD_3; HlyD family secretion protein (PF13437; HMM-score: 16.4)GCV_H; Glycine cleavage H-protein (PF01597; HMM-score: 14.9)no clan defined GP70; Gene 70 protein (PF17429; HMM-score: 12.1)DUF2155; Uncharacterized protein conserved in bacteria (DUF2155) (PF09923; HMM-score: 9.8)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: (R)-lipoate
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- 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): 0.002847
- TAT(Tat/SPI): 0.000164
- LIPO(Sec/SPII): 0.000399
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTSTAKQNQPRNNGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSVDTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVKTRNHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLATKARNKQLTAEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRNMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLENTNIY
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 579 [4]
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 21.83 h [5]
⊟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]
- ↑ 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) - ↑ 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) - ↑ 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) - ↑ 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) - ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)