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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0100 [new locus tag: SACOL_RS00495 ]
- pan locus tag?: SAUPAN000914000
- symbol: SACOL0100
- pan gene symbol?: sbnA
- synonym:
- product: cysteine synthase/cystathionine beta-synthase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0100 [new locus tag: SACOL_RS00495 ]
- symbol: SACOL0100
- product: cysteine synthase/cystathionine beta-synthase
- replicon: chromosome
- strand: +
- coordinates: 113694..114641
- length: 948
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236858 NCBI
- RefSeq: YP_185004 NCBI
- BioCyc: see SACOL_RS00495
- MicrobesOnline: 911579 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901TTGTTAGATTCTGTAGGGCAAACACCTATGGTTCAACTTCATCAACTATTTCCGAAACAT
GAAGTGTTTGCAAAGTTAGAGTATATGAATCCTGGAGGCAGCATGAAAGATCGACCTGCC
AAGTACATCATTGAACATGGTATTAAACATGGTTTAATCACTGAGAATACACATTTAATT
GAAAGTACTTCTGGTAATTTAGGCATTGCGTTGGCAATGATAGCTAAAATCAAGGGATTA
AAACTCACGTGTGTTGTTGATCCTAAAATATCACCAACAAATTTGAAAATTATTAAAAGT
TATGGTGCCAATGTAGAAATGGTTGAAGAACCTGATGCACATGGGGGTTATTTAATGACT
CGTATTGCAAAGGTGCAAGAACTGTTAGCCACTATTGACGATGCATATTGGATTAATCAA
TATGCGAATGAGTTAAATTGGCAATCCCATTATCATGGTGCAGGCACAGAGATTGTTGAA
ACAATTAAGCAACCTATAGATTATTTTGTCGCGCCAGTCAGCACGACAGGTAGCATTATG
GGTATGAGTAGAAAAATAAAAGAAGTGCATCCAAACGCACAAATTGTTGCTGTTGATGCG
AAAGGGTCAGTCATTTTTGGTGACAAACCTATTAATAGAGAATTACCTGGTATCGGTGCT
AGTCGTGTACCCGAAATATTGAATAGATCAGAAATTAATCAAGTGATCCATGTAGATGAT
TATCAATCTGCTTTGGGCTGTCGAAAACTGATTGATTATGAAGGCATATTTGCCGGAGGT
TCAACAGGTTCGATTATTGCAGCGATTGAGCAGTTGATAACGTCAATTGAAGAAGGTGCA
ACAATTGTCACGATTTTACCAGATCGAGGCGATCGTTACTTAGATTTAGTTTATTCAGAT
ACATGGTTAGAAAAAATGAAATCAAGACAAGGAGTTAAATCAGAATGA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0100 [new locus tag: SACOL_RS00495 ]
- symbol: SACOL0100
- description: cysteine synthase/cystathionine beta-synthase
- length: 315
- theoretical pI: 6.18266
- theoretical MW: 34684.6
- GRAVY: -0.129524
⊟Function[edit | edit source]
- TIGRFAM: Cellular processes Biosynthesis of natural products 2,3-diaminopropionate biosynthesis protein SbnA (TIGR03945; HMM-score: 448)and 10 moreAmino acid biosynthesis Serine family cysteine synthase (TIGR01136; EC 2.5.1.47; HMM-score: 259.8)Amino acid biosynthesis Serine family cysteine synthase A (TIGR01139; EC 2.5.1.47; HMM-score: 238.8)Amino acid biosynthesis Serine family cystathionine beta-synthase (TIGR01137; EC 4.2.1.22; HMM-score: 230.2)Amino acid biosynthesis Serine family cysteine synthase B (TIGR01138; EC 2.5.1.47; HMM-score: 214.2)Amino acid biosynthesis Pyruvate family threonine ammonia-lyase (TIGR01127; EC 4.3.1.19; HMM-score: 42.7)Amino acid biosynthesis Aspartate family threonine synthase (TIGR00260; EC 4.2.3.1; HMM-score: 33.4)ectoine utilization protein EutB (TIGR02991; HMM-score: 30.3)Amino acid biosynthesis Pyruvate family threonine ammonia-lyase, biosynthetic (TIGR01124; EC 4.3.1.19; HMM-score: 26.2)Amino acid biosynthesis Aromatic amino acid family tryptophan synthase, beta subunit (TIGR00263; EC 4.2.1.20; HMM-score: 18.1)Amino acid biosynthesis Pyruvate family threonine dehydratase (TIGR02079; EC 4.3.1.19; HMM-score: 18)
- TheSEED :
- N-(2-amino-2-carboxyethyl)-L-glutamate synthase (EC 2.5.1.140)
- PFAM: no clan defined PALP; Pyridoxal-phosphate dependent enzyme (PF00291; HMM-score: 198.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: pyridoxal 5'-phosphate
- 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
- 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): 0.006433
- TAT(Tat/SPI): 0.000287
- LIPO(Sec/SPII): 0.00044
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MLDSVGQTPMVQLHQLFPKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWLEKMKSRQGVKSE
⊟Experimental data[edit | edit source]
- experimentally validated: data available for NCTC8325
- protein localization: Cytoplasmic [1]
- quantitative data / protein copy number per cell:
- interaction partners:
SACOL1199 (ftsZ) cell division protein FtsZ [2] (data from MRSA252) SACOL0593 (fusA) elongation factor G [2] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [2] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [2] (data from MRSA252) SACOL1922 (hemL2) glutamate-1-semialdehyde aminotransferase [2] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [2] (data from MRSA252) SACOL2623 (mqo2) malate:quinone oxidoreductase [2] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [2] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [2] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [2] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [2] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [2] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [2] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [2] (data from MRSA252) SACOL0816 (secA) preprotein translocase subunit SecA [2] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [2] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [2] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [2] (data from MRSA252) SACOL0944 NADH dehydrogenase [2] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [2] (data from MRSA252) SACOL1759 universal stress protein [2] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: Fur* (repression) regulon
Fur* (TF) important in Iron homeostasis; RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟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]
- ↑ 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) - ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 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]
Suzanne E Dale, Amanda Doherty-Kirby, Gilles Lajoie, David E Heinrichs
Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore.
Infect Immun: 2004, 72(1);29-37
[PubMed:14688077] [WorldCat.org] [DOI] (P p)