NCBI date : _
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1103 [new locus tag: SACOL_RS05635 ]
- pan locus tag?: SAUPAN003318000
- symbol: pdhB
- pan gene symbol?: pdhB
- synonym:
- product: pyruvate dehydrogenase complex E1 component subunit beta
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1103 [new locus tag: SACOL_RS05635 ]
- symbol: pdhB
- product: pyruvate dehydrogenase complex E1 component subunit beta
- replicon: chromosome
- strand: +
- coordinates: 1113186..1114163
- length: 978
- 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
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961ATGGCACAAATGACAATGGTTCAAGCGATTAATGATGCGCTTAAAACTGAACTTAAAAAT
GACCAAGATGTTTTAATTTTTGGTGAAGACGTTGGTGTTAACGGCGGTGTTTTCCGTGTT
ACTGAAGGACTACAAAAAGAATTTGGTGAAGATAGAGTATTCGATACACCTTTAGCTGAA
TCAGGTATTGGTGGTTTAGCGATGGGTCTTGCAGTTGAAGGATTCCGTCCGGTTATGGAA
GTACAATTCTTAGGTTTCGTATTCGAAGTATTTGATGCGATTGCTGGACAAATTGCACGT
ACTCGTTTCCGTTCAGGCGGTACTAAAACTGCACCTGTAACAATTCGTGGACCATTTGGT
GGTGGCGTACACACACCAGAATTACACGCAGATAACTTAGAAGGTATTTTAGCTCAATCT
CCAGGTCTAAAGGTTGTTATTCCTTCAGGCCCATACGATGCGAAAGGTTTATTAATTTCT
TCTATTAGAAGTAATGACCCAGTCGTATACTTAGAGCATATGAAATTGTATCGTTCATTC
CGTGAAGAAGTACCTGAAGAAGAATATACAATTGACATTGGTAAGGCTAATGTGAAAAAA
GAAGGTAATGACATTTCAATCATCACATACGGTGCAATGGTTCAAGAATCAATGAAAGCT
GCAGAAGAACTTGAAAAAGATGGTTATTCTGTTGAAGTAATTGACTTACGTACTGTTCAA
CCAATCGATGTTGACACAATTGTAGCTTCAGTTGAAAAAACTGGTCGTGCAGTTGTAGTT
CAAGAAGCACAACGTCAAGCTGGTGTTGGTGCAGCAGTTGTAGCTGAATTAAGTGAACGT
GCAATCCTTTCATTAGAAGCACCTATTGGAAGAGTTGCAGCAGCAGATACAATTTATCCA
TTCACTCAAGCTGAAAATGTTTGGTTACCAAACAAAAATGACATCATCGAAAAAGCAAAA
GAAACTTTAGAATTTTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1103 [new locus tag: SACOL_RS05635 ]
- symbol: PdhB
- description: pyruvate dehydrogenase complex E1 component subunit beta
- length: 325
- theoretical pI: 4.36436
- theoretical MW: 35215.8
- GRAVY: -0.0455385
⊟Function[edit | edit source]
- reaction: EC 1.2.4.1? ExPASyPyruvate dehydrogenase (acetyl-transferring) Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
- TIGRFAM: Biosynthesis of cofactors, prosthetic groups, and carriers Other 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83.1)Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83.1)Biosynthesis of cofactors, prosthetic groups, and carriers Pyridoxine 1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83.1)and 2 more2-oxoacid:acceptor oxidoreductase, alpha subunit (TIGR03710; HMM-score: 25.6)pyruvate:ferredoxin (flavodoxin) oxidoreductase (TIGR02176; EC 1.2.7.1; HMM-score: 10.5)
- TheSEED :
- Pyruvate dehydrogenase E1 component beta subunit (EC 1.2.4.1)
Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes Pyruvate dehydrogenase E1 component beta subunit (EC 1.2.4.1)and 1 more - PFAM: TKC_like (CL0591) Transketolase_C; Transketolase, C-terminal domain (PF02780; HMM-score: 135.3)THDP-binding (CL0254) Transket_pyr; Transketolase, pyrimidine binding domain (PF02779; HMM-score: 130.4)and 1 moreTKC_like (CL0591) PFOR_II; Pyruvate:ferredoxin oxidoreductase core domain II (PF17147; HMM-score: 18.3)
⊟Structure, modifications & interactions[edit | edit source]
- domains:
- modifications:
- cofactors: thiamine diphosphate
- effectors:
- interaction partners:
SACOL2657 (arcA) arginine deiminase [1] (data from MRSA252) SACOL1721 (clpX) ATP-dependent protease ATP-binding subunit ClpX [1] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [1] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [1] (data from MRSA252) SACOL0593 (fusA) elongation factor G [1] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [1] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [1] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [1] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [1] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [1] (data from MRSA252) SACOL1477 (ilvA1) threonine dehydratase [1] (data from MRSA252) SACOL2092 (murAA) UDP-N-acetylglucosamine 1-carboxyvinyltransferase [1] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [1] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [1] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [1] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [1] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [1] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [1] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [1] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [1] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [1] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [1] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [1] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [1] (data from MRSA252) SACOL1725 (rplT) 50S ribosomal protein L20 [1] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [1] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [1] (data from MRSA252) SACOL2237 (rplW) 50S ribosomal protein L23 [1] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [1] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [1] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [1] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [1] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [1] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [1] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [1] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [1] (data from MRSA252) SACOL0435 GTP-dependent nucleic acid-binding protein EngD [1] (data from MRSA252) SACOL0944 NADH dehydrogenase [1] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [1] (data from MRSA252) SACOL1759 universal stress protein [1] (data from MRSA252) SACOL2114 aldehyde dehydrogenase [1] (data from MRSA252) SACOL2553 pyruvate oxidase [1] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [1] (data from MRSA252)
⊟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
- 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): 0.004498
- TAT(Tat/SPI): 0.000165
- LIPO(Sec/SPII): 0.000333
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRGPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
⊟Peptides[edit | edit source]
- experimentally validated: PeptideAtlas
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: pdhA > pdhB > pdhC > pdhD
⊟Regulation[edit | edit source]
- sigma factors : _
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Stability[edit | edit source]
- half-life: 22.2 h [2]
⊟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]
- ↑ 1.00 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 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 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) - ↑ 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)