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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL2004 [new locus tag: SACOL_RS10475 ]
- pan locus tag?: SAUPAN005190000
- symbol: SACOL2004
- pan gene symbol?: lukG
- synonym: lukB
- product: leukocidin subunit precursor
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL2004 [new locus tag: SACOL_RS10475 ]
- symbol: SACOL2004
- product: leukocidin subunit precursor
- replicon: chromosome
- strand: -
- coordinates: 2064956..2065828
- length: 873
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3238002 NCBI
- RefSeq: YP_186827 NCBI
- BioCyc: see SACOL_RS10475
- MicrobesOnline: 913481 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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841ATGTATACACGTACAGCTACAACAAGTGATAGTCAAAAAAATATTACTCAAAGCTTACAA
TTTAATTTCTTAACTGAACCTAATTATGATAAAGAAACAGTATTTATTAAAGCAAAAGGT
ACAATTGGTAGTGGTTTGAGAATTTTAGACCCAAATGGTTATTGGAATAGTACATTAAGA
TGGCCTGGATCTTATTCAGTTTCAATTCAAAATGTTGATGACAACAACAATACAAATGTG
ACTGACTTTGCACCAAAAAATCAGGATGAATCAAGAGAAGTTAAATATACGTATGGTTAT
AAAACAGGTGGAGATTTTTCGATTAATCGTGGAGGCTTAACTGGAAATATTACAAAAGAG
AGTAATTATTCAGAGACGATTAGTTATCAACAACCATCATATCGTACATTACTTGATCAA
TCTACGTCACATAAAGGTGTAGGTTGGAAAGTAGAAGCACATTTGATAAATAATATGGGA
CATGACCATACGAGACAATTAACTAATGATAGTGATAATAGAACTAAAAGTGAAATTTTT
TCTTTAACACGAAATGGAAATTTATGGGCGAAAGATAATTTCACACCTAAAGACAAAATG
CCTGTAACTGTGTCTGAAGGGTTTAATCCAGAATTTTTAGCTGTTATGTCACATGATAAA
AAAGACAAAGGTAAATCACAATTTGTTGTTCATTATAAAAGATCAATGGATGAGTTTAAA
ATAGATTGGAATCGCCATGGTTTCTGGGGCTATTGGTCTGGTGAAAACCATGTAGATAAA
AAAGAAGAAAAATTATCAGCATTATATGAAGTTGATTGGAAGACACATAATGTGAAGTTT
GTAAAAGTACTTAATGATAATGAAAAGAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL2004 [new locus tag: SACOL_RS10475 ]
- symbol: SACOL2004
- description: leukocidin subunit precursor
- length: 290
- theoretical pI: 8.97618
- theoretical MW: 33444.7
- GRAVY: -0.995517
⊟Function[edit | edit source]
- TIGRFAM: Cellular processes Toxin production and resistance beta-channel forming cytolysin (TIGR01002; HMM-score: 247.6)and 2 moreCell envelope Surface structures type IVB pilus formation outer membrane protein, R64 PilN family (TIGR02520; HMM-score: 11.1)Protein fate Protein and peptide secretion and trafficking type IVB pilus formation outer membrane protein, R64 PilN family (TIGR02520; HMM-score: 11.1)
- TheSEED :
- Cytolytic pore-forming protein => Leukocidin LukF-G
- PFAM: Leukocidin (CL0636) Leukocidin; Leukocidin/Hemolysin toxin family (PF07968; HMM-score: 294.6)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Extracellular
- Cytoplasmic Score: 0.01
- Cytoplasmic Membrane Score: 0.09
- Cellwall Score: 0.18
- Extracellular Score: 9.72
- 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): 0.018407
- TAT(Tat/SPI): 0.001504
- LIPO(Sec/SPII): 0.001343
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MYTRTATTSDSQKNITQSLQFNFLTEPNYDKETVFIKAKGTIGSGLRILDPNGYWNSTLRWPGSYSVSIQNVDDNNNTNVTDFAPKNQDESREVKYTYGYKTGGDFSINRGGLTGNITKESNYSETISYQQPSYRTLLDQSTSHKGVGWKVEAHLINNMGHDHTRQLTNDSDNRTKSEIFSLTRNGNLWAKDNFTPKDKMPVTVSEGFNPEFLAVMSHDKKDKGKSQFVVHYKRSMDEFKIDWNRHGFWGYWSGENHVDKKEEKLSALYEVDWKTHNVKFVKVLNDNEKK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell:
- interaction partners:
SACOL1760 (ackA) acetate kinase [4] (data from MRSA252) SACOL1385 (acnA) aconitate hydratase [4] (data from MRSA252) SACOL0452 (ahpC) alkyl hydroperoxide reductase subunit C [4] (data from MRSA252) SACOL2657 (arcA) arginine deiminase [4] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [4] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [4] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SACOL0634 (eutD) phosphotransacetylase [4] (data from MRSA252) SACOL2117 (fbaA) fructose-bisphosphate aldolase [4] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [4] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [4] (data from MRSA252) SACOL1782 (fhs) formate--tetrahydrofolate ligase [4] (data from MRSA252) SACOL0593 (fusA) elongation factor G [4] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [4] (data from MRSA252) SACOL2016 (groEL) chaperonin GroEL [4] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [4] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [4] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [4] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [4] (data from MRSA252) SACOL2618 (ldh2) L-lactate dehydrogenase [4] (data from MRSA252) SACOL0562 (lysS) lysyl-tRNA synthetase [4] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [4] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [4] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [4] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [4] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [4] (data from MRSA252) SACOL1982 (ppaC) manganese-dependent inorganic pyrophosphatase [4] (data from MRSA252) SACOL0544 (prsA) ribose-phosphate pyrophosphokinase [4] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [4] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [4] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [4] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [4] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [4] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [4] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [4] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [4] (data from MRSA252) SACOL2207 (rplM) 50S ribosomal protein L13 [4] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [4] (data from MRSA252) SACOL1516 (rpsA) 30S ribosomal protein S1 [4] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [4] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [4] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [4] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [4] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [4] (data from MRSA252) SACOL2225 (rpsH) 30S ribosomal protein S8 [4] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [4] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [4] (data from MRSA252) SACOL1254 (rpsP) 30S ribosomal protein S16 [4] (data from MRSA252) SACOL0439 (rpsR) 30S ribosomal protein S18 [4] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [4] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [4] (data from MRSA252) SACOL1262 (sucC) succinyl-CoA synthetase subunit beta [4] (data from MRSA252) SACOL1831 (tal) translaldolase [4] (data from MRSA252) SACOL1722 (tig) trigger factor [4] (data from MRSA252) SACOL1377 (tkt) transketolase [4] (data from MRSA252) SACOL0840 (tpiA) triosephosphate isomerase [4] (data from MRSA252) SACOL1155 (trxA) thioredoxin [4] (data from MRSA252) SACOL1276 (tsf) elongation factor Ts [4] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [4] (data from MRSA252) SACOL0303 5'-nucleotidase [4] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [4] (data from MRSA252) SACOL0688 ABC transporter substrate-binding protein [4] (data from MRSA252) SACOL0944 NADH dehydrogenase [4] (data from MRSA252) SACOL1952 ferritins family protein [4] (data from MRSA252) SACOL2173 alkaline shock protein 23 [4] (data from MRSA252) SACOL2296 glycerate dehydrogenase [4] (data from MRSA252) SACOL2553 pyruvate oxidase [4] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟Regulation[edit | edit source]
- regulator: SaeR (activation) regulon
SaeR (TF) important in Virulence; RegPrecise transcription unit transferred from N315 data 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]
- ↑ 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, 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) - ↑ 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) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 4.46 4.47 4.48 4.49 4.50 4.51 4.52 4.53 4.54 4.55 4.56 4.57 4.58 4.59 4.60 4.61 4.62 4.63 4.64 4.65 4.66 4.67 4.68 4.69 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]
Stephan Fuchs, Jan Pané-Farré, Christian Kohler, Michael Hecker, Susanne Engelmann
Anaerobic gene expression in Staphylococcus aureus.
J Bacteriol: 2007, 189(11);4275-89
[PubMed:17384184] [WorldCat.org] [DOI] (P p)S J Projan, J Kornblum, B Kreiswirth, S L Moghazeh, W Eisner, R P Novick
Nucleotide sequence: the beta-hemolysin gene of Staphylococcus aureus.
Nucleic Acids Res: 1989, 17(8);3305
[PubMed:2726469] [WorldCat.org] [DOI] (P p)