From AureoWiki
Revision as of 13:40, 11 March 2016 by AureoSysAdmin (talk | contribs) (Text replacement - "gene Genbank" to "gene RefSeq")
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1721 [new locus tag: SACOL_RS08790 ]
  • pan locus tag?: SAUPAN004290000
  • symbol: clpX
  • pan gene symbol?: clpX
  • synonym:
  • product: ATP-dependent protease ATP-binding subunit ClpX

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1721 [new locus tag: SACOL_RS08790 ]
  • symbol: clpX
  • product: ATP-dependent protease ATP-binding subunit ClpX
  • replicon: chromosome
  • strand: -
  • coordinates: 1751834..1753096
  • length: 1263
  • 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
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    ATGTTTAAATTCAATGAAGATGAAGAAAATTTGAAATGCTCTTTCTGCGGAAAAGACCAA
    GATCAAGTAAAAAAACTTGTAGCAGGAAGTGGTGTATATATTTGTAATGAGTGTATTGAA
    TTATGCTCAGAAATCGTCGAAGAAGAATTAGCTCAAAACACTTCTGAAGCGATGACAGAA
    TTACCTACTCCTAAAGAAATTATGGATCATTTAAACGAATATGTTATTGGTCAAGAAAAA
    GCTAAAAAATCTTTAGCTGTAGCTGTTTATAACCACTATAAGCGTATTCAACAATTAGGA
    CCAAAAGAAGATGATGTTGAATTACAAAAAAGTAACATTGCATTAATTGGGCCAACAGGT
    AGTGGTAAAACATTATTAGCTCAAACCTTAGCCAAGACGTTGAATGTACCATTTGCAATT
    GCAGATGCGACAAGTTTAACTGAAGCTGGTTATGTAGGCGATGATGTTGAAAATATCTTG
    TTGAGATTAATTCAAGCAGCTGACTTTGACATTGATAAAGCCGAAAAAGGTATTATTTAT
    GTAGATGAAATTGATAAAATTGCACGTAAATCTGAAAACACATCTATAACACGTGACGTT
    TCAGGTGAAGGTGTTCAACAAGCATTGCTTAAAATCTTAGAAGGTACGACTGCAAGTGTT
    CCGCCACAAGGTGGACGCAAACATCCAAACCAAGAAATGATTCAAATTGATACAACAAAT
    ATCTTATTTATTCTTGGTGGTGCCTTTGATGGTATTGAAGAAGTGATTAAGCGCCGTCTT
    GGTGAAAAAGTTATTGGTTTCTCAAGCAATGAAGCTGATAAATATGACGAACAAGCATTA
    TTAGCACAAATTCGCCCAGAAGATTTGCAAGCCTATGGTTTGATTCCTGAATTTATCGGA
    CGTGTGCCAATTGTAGCTAATTTAGAAACATTAGATGTAACTGCGTTGAAAAACATCTTA
    ACGCAACCTAAAAATGCACTTGTGAAACAATATACTAAAATGCTGGAATTAGATGATGTG
    GATTTAGAGTTCACTGAAGAAGCTTTATCAGCAATTAGTGAAAAAGCAATTGAAAGAAAA
    ACAGGTGCGCGTGGTTTACGTTCAATCATAGAAGAATCGTTAATCGATATTATGTTTGAT
    GTGCCTTCTAACGAAAATGTAACGAAGGTAGTTATTACAGCACAAACAATTAATGAAGAA
    ACTGAACCAGAACTATACGACGCAGAAGGCAATTTAATTAATAATAGTAAAACATCAGCT
    TAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1263

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1721 [new locus tag: SACOL_RS08790 ]
  • symbol: ClpX
  • description: ATP-dependent protease ATP-binding subunit ClpX
  • length: 420
  • theoretical pI: 4.26448
  • theoretical MW: 46297.2
  • GRAVY: -0.265238

⊟Function[edit | edit source]

  • ⊞TIGRFAM:
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides ATP-dependent Clp protease, ATP-binding subunit ClpX (TIGR00382; HMM-score: 660.9)
    Genetic information processing Protein fate Protein folding and stabilization ATP-dependent Clp protease, ATP-binding subunit ClpX (TIGR00382; HMM-score: 660.9)
    and 25 more
    Genetic information processing Protein fate Protein folding and stabilization ATP-dependent protease HslVU, ATPase subunit (TIGR00390; HMM-score: 212.6)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides ATP-dependent Clp protease ATP-binding subunit ClpA (TIGR02639; HMM-score: 46.1)
    Genetic information processing Protein fate Protein folding and stabilization ATP-dependent chaperone protein ClpB (TIGR03346; HMM-score: 36.9)
    Cellular processes Cellular processes Pathogenesis type VI secretion ATPase, ClpV1 family (TIGR03345; HMM-score: 36.2)
    Genetic information processing Protein fate Protein and peptide secretion and trafficking type VI secretion ATPase, ClpV1 family (TIGR03345; HMM-score: 36.2)
    AAA family ATPase, CDC48 subfamily (TIGR01243; HMM-score: 31.4)
    26S proteasome subunit P45 family (TIGR01242; HMM-score: 30)
    Cellular processes Cellular processes Cell division ATP-dependent metallopeptidase HflB (TIGR01241; EC 3.4.24.-; HMM-score: 27.4)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides ATP-dependent metallopeptidase HflB (TIGR01241; EC 3.4.24.-; HMM-score: 27.4)
    Genetic information processing DNA metabolism DNA replication, recombination, and repair Holliday junction DNA helicase RuvB (TIGR00635; EC 3.6.4.12; HMM-score: 25.4)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides endopeptidase La (TIGR00763; EC 3.4.21.53; HMM-score: 23.8)
    Cellular processes Cellular processes Chemotaxis and motility flagellar biosynthesis protein FlhF (TIGR03499; HMM-score: 23.2)
    Unknown function General Mg chelatase-like protein (TIGR00368; HMM-score: 22.2)
    nicotinamide-nucleotide adenylyltransferase (TIGR01526; EC 2.7.7.1; HMM-score: 21.3)
    Cellular processes Cellular processes Other gas vesicle protein GvpN (TIGR02640; HMM-score: 20.1)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides putative ATP-dependent protease (TIGR00764; HMM-score: 16.9)
    Hypothetical proteins Conserved TIGR00270 family protein (TIGR00270; HMM-score: 16.5)
    Genetic information processing DNA metabolism DNA replication, recombination, and repair orc1/cdc6 family replication initiation protein (TIGR02928; HMM-score: 15.8)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Nucleotide and nucleoside interconversions cytidylate kinase (TIGR00017; EC 2.7.4.14; HMM-score: 14.5)
    Genetic information processing Protein fate Protein and peptide secretion and trafficking type VII secretion AAA-ATPase EccA (TIGR03922; HMM-score: 13.1)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA dimethylallyltransferase (TIGR00174; EC 2.5.1.75; HMM-score: 12.8)
    Metabolism Transport and binding proteins Anions phosphate ABC transporter, ATP-binding protein (TIGR00972; EC 3.6.3.27; HMM-score: 12.8)
    thiol reductant ABC exporter, CydC subunit (TIGR02868; HMM-score: 12.8)
    Metabolism Transport and binding proteins Anions sulfate ABC transporter, ATP-binding protein (TIGR00968; EC 3.6.3.25; HMM-score: 12.1)
    carbohydrate kinase, thermoresistant glucokinase family (TIGR01313; EC 2.7.1.-; HMM-score: 12.1)
  • ⊞TheSEED  :
    • ATP-dependent Clp protease ATP-binding subunit ClpX
    Protein Metabolism Protein degradation Proteasome bacterial  ATP-dependent Clp protease ATP-binding subunit ClpX
    and 1 more
    Protein Metabolism Protein degradation Proteolysis in bacteria, ATP-dependent  ATP-dependent Clp protease ATP-binding subunit ClpX
  • ⊞PFAM:
    P-loop_NTPase (CL0023) AAA_2; AAA domain (Cdc48 subfamily) (PF07724; HMM-score: 117.1)
    and 29 more
    Zn_Beta_Ribbon (CL0167) zf-C4_ClpX; ClpX C4-type zinc finger (PF06689; HMM-score: 67.7)
    P-loop_NTPase (CL0023) AAA; ATPase family associated with various cellular activities (AAA) (PF00004; HMM-score: 61.1)
    AAA_lid (CL0671) ClpB_D2-small; C-terminal, D2-small domain, of ClpB protein (PF10431; HMM-score: 47.6)
    P-loop_NTPase (CL0023) AAA_5; AAA domain (dynein-related subfamily) (PF07728; HMM-score: 28.2)
    AAA_22; AAA domain (PF13401; HMM-score: 27)
    RuvB_N; Holliday junction DNA helicase RuvB P-loop domain (PF05496; HMM-score: 26.2)
    Mg_chelatase; Magnesium chelatase, subunit ChlI (PF01078; HMM-score: 22.4)
    MCM; MCM P-loop domain (PF00493; HMM-score: 21.4)
    AAA_18; AAA domain (PF13238; HMM-score: 19.5)
    Sigma54_activ_2; Sigma-54 interaction domain (PF14532; HMM-score: 19.3)
    Sigma54_activat; Sigma-54 interaction domain (PF00158; HMM-score: 18.7)
    AAA_14; AAA domain (PF13173; HMM-score: 18)
    ABC_tran; ABC transporter (PF00005; HMM-score: 17.9)
    TsaE; Threonylcarbamoyl adenosine biosynthesis protein TsaE (PF02367; HMM-score: 17.9)
    IstB_IS21; IstB-like ATP binding protein (PF01695; HMM-score: 17.2)
    AAA_16; AAA ATPase domain (PF13191; HMM-score: 17)
    AAA_17; AAA domain (PF13207; HMM-score: 16.3)
    NACHT; NACHT domain (PF05729; HMM-score: 16)
    AAA_28; AAA domain (PF13521; HMM-score: 15.9)
    nSTAND3; Novel STAND NTPase 3 (PF20720; HMM-score: 15.5)
    ResIII; Type III restriction enzyme, res subunit (PF04851; HMM-score: 14.8)
    AAA_24; AAA domain (PF13479; HMM-score: 14.5)
    AAA_7; P-loop containing dynein motor region (PF12775; HMM-score: 14)
    Cytidylate_kin; Cytidylate kinase (PF02224; HMM-score: 13.8)
    DEAD; DEAD/DEAH box helicase (PF00270; HMM-score: 13.6)
    RNA_helicase; RNA helicase (PF00910; HMM-score: 13.5)
    AAA_33; AAA domain (PF13671; HMM-score: 13.1)
    PduV-EutP; Ethanolamine utilisation - propanediol utilisation (PF10662; HMM-score: 12.7)
    RING (CL0229) C1_2; C1 domain (PF03107; HMM-score: 11.3)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • 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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9758
    • Cytoplasmic Membrane Score: 0.0144
    • Cell wall & surface Score: 0.0008
    • Extracellular Score: 0.009
  • ⊞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): 0.063176
    • TAT(Tat/SPI): 0.001019
    • LIPO(Sec/SPII): 0.00183
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MFKFNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAMTELPTPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLRLIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNILFILGGAFDGIEEVIKRRLGEKVIGFSSNEADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINEETEPELYDAEGNLINNSKTSA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1882 [5]
  • ⊟interaction partners:
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL0211acetyl-CoA acetyltransferase  [6] (data from MRSA252)
    SACOL0508hypothetical protein  [6] (data from MRSA252)
    SACOL2297hypothetical protein  [6] (data from MRSA252)
    SACOL2553pyruvate oxidase  [6] (data from MRSA252)
    SACOL2582hypothetical protein  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 10.02 h [7]

⊞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. ↑ 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)
  2. ↑ 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ Jump up to: 6.0 6.1 6.2 6.3 6.4 6.5 6.6 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)
  7. ↑ 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)

⊟Relevant publications[edit | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SACOL1721&oldid=101649"