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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01226
- pan locus tag?: SAUPAN003552000
- symbol: hslU
- pan gene symbol?: hslU
- synonym: clpY
- product: ATP-dependent protease ATP-binding subunit HslU
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01226
- symbol: hslU
- product: ATP-dependent protease ATP-binding subunit HslU
- replicon: chromosome
- strand: +
- coordinates: 1178277..1179680
- length: 1404
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3920254 NCBI
- RefSeq: YP_499762 NCBI
- BioCyc: G1I0R-1148 BioCyc
- MicrobesOnline: 1289676 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1381ATGGATACAGCTGGAATAAGATTAACTCCAAAAGAAATCGTATCTAAATTAAATGAATAC
ATCGTTGGACAAAATGATGCTAAACGTAAAGTGGCAATTGCCCTACGTAATCGATACAGA
AGAAGTTTATTAGATGAGGAATCAAAGCAAGAAATTTCACCTAAAAATATTTTGATGATT
GGACCAACCGGCGTTGGTAAAACTGAAATTGCAAGAAGAATGGCCAAAGTTGTCGGCGCG
CCATTTATAAAAGTAGAAGCTACTAAATTTACTGAGGTAGGTTATGTAGGACGAGATGTT
GAAAGTATGGTTAGAGATCTTGTTGATGTTTCAGTAAGATTAGTCAAGGCGCAGAAAAAA
TCATTGGTACAAGATGAAGCAACAGCTAAGGCCAATGAAAAACTTGTTAAGTTATTAGTT
CCAAGTATGAAAAAGAAAGCGTCTCAAACGAATAATCCTTTAGAGTCACTTTTCGGAGGT
GCAATTCCAAATTTCGGACAAAATAACGAAGATGAAGAAGAACCACCTACTGAGGAAATT
AAAACAAAACGTTCTGAAATTAAGAGACAGCTAGAAGAAGGCAAACTTGAAAAAGAAAAG
GTAAGAATTAAAGTCGAACAAGATCCTGGTGCTTTAGGTATGCTAGGTACAAATCAAAAT
CAGCAAATGCAAGAGATGATGAATCAATTAATGCCTAAAAAGAAAGTTGAGCGAGAAGTT
GCTGTTGAGACGGCAAGGAAAATCTTAGCTGATAGTTATGCGGATGAACTAATTGATCAA
GAAAGCGCTAACCAAGAAGCGCTTGAATTAGCAGAACAAATGGGTATCATCTTTATAGAT
GAAATCGACAAAGTTGCGACGAATAATCATAATAGTGGTCAAGATGTCTCAAGACAAGGT
GTTCAAAGAGATATTTTACCTATACTTGAAGGTAGCGTTATTCAAACCAAATATGGTACT
GTGAATACTGAACATATGCTGTTTATAGGTGCTGGAGCTTTCCATGTATCTAAGCCGAGT
GACTTGATACCAGAATTGCAAGGTCGTTTTCCGATTAGAGTTGAACTTGATAGTTTATCG
GTAGAAGATTTTGTAAGAATTTTGACAGAACCAAAATTGTCATTAATTAAACAATATGAA
GCATTGCTTCAAACAGAAGAAGTTACTGTAAACTTTACCGATGAAGCAATTACTCGCTTA
GCTGAGATTGCTTATCAAGTAAATCAAGATACAGACAACATTGGTGCACGTCGACTTCAT
ACAATTTTAGAAAAGATGCTAGAAGATTTATCATTCGAAGCACCAAGTATGCCGAATGCA
GTTGTAGATATTACCCCACAATATGTTGATGATAAATTAAAATCAATTTCAACAAATAAA
GATTTAAGTGCATTTATTCTATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01226
- symbol: HslU
- description: ATP-dependent protease ATP-binding subunit HslU
- length: 467
- theoretical pI: 4.95489
- theoretical MW: 52314.5
- GRAVY: -0.428266
⊟Function[edit | edit source]
- ⊞TIGRFAM: Protein fate Protein folding and stabilization ATP-dependent protease HslVU, ATPase subunit (TIGR00390; HMM-score: 621)and 18 more
- ⊞TheSEED :
- ATP-dependent hsl protease ATP-binding subunit HslU
Protein Metabolism Protein degradation Proteasome bacterial ATP-dependent hsl protease ATP-binding subunit HslUand 1 more - ⊞PFAM: P-loop_NTPase (CL0023) AAA_2; AAA domain (Cdc48 subfamily) (PF07724; HMM-score: 110.5)and 30 more
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MDTAGIRLTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPLESLFGGAIPNFGQNNEDEEEPPTEEIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGALGMLGTNQNQQMQEMMNQLMPKKKVEREVAVETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVNTEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEIAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- ⊟interaction partners:
SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_00002 DNA polymerase III subunit beta [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01653 superoxide dismutase [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01867 D-alanine aminotransferase [3] (data from MRSA252) SAOUHSC_02337 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SAOUHSC_01224 > SAOUHSC_01225 > hslU > SAOUHSC_01228predicted SigA promoter [4] : SAOUHSC_01222 > S504 > SAOUHSC_01223 > S505 > SAOUHSC_01224 > SAOUHSC_01225 > hslU > SAOUHSC_01228 > S506 > SAOUHSC_01230 > S507 > S508 > rpsB > SAOUHSC_01233 > tsf > S509 > pyrH > frr > S510 > S511 > SAOUHSC_01237 > SAOUHSC_01238 > S512 > SAOUHSC_01239 > SAOUHSC_01240predicted SigA promoter [4] : SAOUHSC_01224 > SAOUHSC_01225 > hslU > SAOUHSC_01228 > S506 > SAOUHSC_01230 > S507
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] ⊟Multi-gene expression profiles
⊟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]
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ Jump up to: 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 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) - ↑ Jump up to: 4.0 4.1 4.2 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)