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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411).UniRule annotation3 Publications

Catalytic activityi

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).UniRule annotation

Enzyme regulationi

Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK).1 Publication

Kineticsi

  1. KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-succinyl-Leu-Tyr-AMC)2 Publications
  2. KM=1.0 mM for N-succinyl-Leu-Tyr-AMC2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei111 – 1111NucleophileCurated
    Active sitei136 – 1361Curated
    Active sitei185 – 1851Curated

    GO - Molecular functioni

    • ATP-dependent peptidase activity Source: CACAO
    • identical protein binding Source: IntAct
    • serine-type endopeptidase activity Source: UniProtKB-HAMAP
    • serine-type peptidase activity Source: EcoCyc

    GO - Biological processi

    • misfolded or incompletely synthesized protein catabolic process Source: MGI
    • proteasomal protein catabolic process Source: CACAO
    • response to heat Source: EcoliWiki
    • response to temperature stimulus Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10158-MONOMER.
    ECOL316407:JW0427-MONOMER.
    MetaCyc:EG10158-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent Clp protease proteolytic subunitUniRule annotation (EC:3.4.21.92UniRule annotation)
    Alternative name(s):
    Caseinolytic protease
    Endopeptidase ClpUniRule annotation
    Heat shock protein F21.5
    Protease Ti
    Gene namesi
    Name:clpPUniRule annotation
    Synonyms:lopP
    Ordered Locus Names:b0437, JW0427
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10158. clpP.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization (PubMed:22412352). Decreased persister cell formation upon antibotic challenge probably due to increased levels of MazF toxin (PubMed:24375411).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171V → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi18 – 181P → A: Reduced processing, no ClpA-ClpP complex forms. 1 Publication
    Mutagenesisi19 – 191M → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi20 – 201V → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi21 – 211I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi24 – 241T → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi27 – 271G → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi32 – 321D → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi33 – 331I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi34 – 341Y → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi126 – 1261F → A: Little ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi185 – 1851D → A: Loss of protease activity, forms ClpA-ClpP complex. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 14141 PublicationPRO_0000268012Add
    BLAST
    Chaini15 – 207193ATP-dependent Clp protease proteolytic subunitPRO_0000179551Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiP0A6G7.
    PRIDEiP0A6G7.

    2D gel databases

    SWISS-2DPAGEP0A6G7.

    Expressioni

    Inductioni

    By heat shock. Part of the clpP-clpX operon.1 Publication

    Interactioni

    Subunit structurei

    Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Component of the ClpAP and ClpXP complexes.UniRule annotation5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-370625,EBI-370625
    clpAP0ABH93EBI-370625,EBI-546140

    Protein-protein interaction databases

    DIPiDIP-31838N.
    IntActiP0A6G7. 67 interactions.
    STRINGi511145.b0437.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 213Combined sources
    Beta strandi22 – 243Combined sources
    Beta strandi27 – 293Combined sources
    Beta strandi30 – 323Combined sources
    Helixi33 – 386Combined sources
    Turni39 – 413Combined sources
    Beta strandi42 – 498Combined sources
    Helixi51 – 6717Combined sources
    Beta strandi69 – 713Combined sources
    Beta strandi73 – 797Combined sources
    Helixi84 – 9613Combined sources
    Beta strandi97 – 993Combined sources
    Beta strandi101 – 11010Combined sources
    Helixi112 – 1187Combined sources
    Beta strandi125 – 1273Combined sources
    Beta strandi132 – 1354Combined sources
    Beta strandi139 – 1457Combined sources
    Helixi146 – 17126Combined sources
    Helixi175 – 1817Combined sources
    Turni182 – 1854Combined sources
    Beta strandi186 – 1894Combined sources
    Helixi190 – 1956Combined sources
    Beta strandi198 – 2025Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TYFX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG8X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b18-207[»]
    2FZSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    3HLNX-ray3.201/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z15-207[»]
    3MT6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-207[»]
    ProteinModelPortaliP0A6G7.
    SMRiP0A6G7. Positions 16-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6G7.

    Family & Domainsi

    Domaini

    The N-terminus (residues 17-34) interact with ClpA and ClpX.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase S14 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0740.
    HOGENOMiHOG000285833.
    InParanoidiP0A6G7.
    KOiK01358.
    OMAiARMNELM.
    OrthoDBiEOG6Z3KQ0.
    PhylomeDBiP0A6G7.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_AS.
    [Graphical view]
    PANTHERiPTHR10381. PTHR10381. 1 hit.
    PfamiPF00574. CLP_protease. 1 hit.
    [Graphical view]
    PRINTSiPR00127. CLPPROTEASEP.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00493. clpP. 1 hit.
    PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6G7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE
    60 70 80 90 100
    DHMANLIVAQ MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD
    110 120 130 140 150
    VSTICMGQAA SMGAFLLTAG AKGKRFCLPN SRVMIHQPLG GYQGQATDIE
    160 170 180 190 200
    IHAREILKVK GRMNELMALH TGQSLEQIER DTERDRFLSA PEAVEYGLVD

    SILTHRN
    Length:207
    Mass (Da):23,187
    Last modified:March 29, 2005 - v1
    Checksum:iA7843D036C8CB3C2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05534 Genomic DNA. Translation: AAA23588.1.
    U82664 Genomic DNA. Translation: AAB40193.1.
    U00096 Genomic DNA. Translation: AAC73540.1.
    AP009048 Genomic DNA. Translation: BAE76217.1.
    PIRiB36575.
    RefSeqiNP_414971.1. NC_000913.3.
    WP_000122253.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73540; AAC73540; b0437.
    BAE76217; BAE76217; BAE76217.
    GeneIDi945082.
    KEGGieco:b0437.
    PATRICi32116027. VBIEscCol129921_0455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05534 Genomic DNA. Translation: AAA23588.1.
    U82664 Genomic DNA. Translation: AAB40193.1.
    U00096 Genomic DNA. Translation: AAC73540.1.
    AP009048 Genomic DNA. Translation: BAE76217.1.
    PIRiB36575.
    RefSeqiNP_414971.1. NC_000913.3.
    WP_000122253.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TYFX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG8X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b18-207[»]
    2FZSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    3HLNX-ray3.201/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z15-207[»]
    3MT6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-207[»]
    ProteinModelPortaliP0A6G7.
    SMRiP0A6G7. Positions 16-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-31838N.
    IntActiP0A6G7. 67 interactions.
    STRINGi511145.b0437.

    2D gel databases

    SWISS-2DPAGEP0A6G7.

    Proteomic databases

    PaxDbiP0A6G7.
    PRIDEiP0A6G7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73540; AAC73540; b0437.
    BAE76217; BAE76217; BAE76217.
    GeneIDi945082.
    KEGGieco:b0437.
    PATRICi32116027. VBIEscCol129921_0455.

    Organism-specific databases

    EchoBASEiEB0156.
    EcoGeneiEG10158. clpP.

    Phylogenomic databases

    eggNOGiCOG0740.
    HOGENOMiHOG000285833.
    InParanoidiP0A6G7.
    KOiK01358.
    OMAiARMNELM.
    OrthoDBiEOG6Z3KQ0.
    PhylomeDBiP0A6G7.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10158-MONOMER.
    ECOL316407:JW0427-MONOMER.
    MetaCyc:EG10158-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A6G7.
    PROiP0A6G7.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_AS.
    [Graphical view]
    PANTHERiPTHR10381. PTHR10381. 1 hit.
    PfamiPF00574. CLP_protease. 1 hit.
    [Graphical view]
    PRINTSiPR00127. CLPPROTEASEP.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00493. clpP. 1 hit.
    PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli."
      Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S.
      J. Biol. Chem. 265:12536-12545(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-36.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5."
      Kroh H.E., Simon L.D.
      J. Bacteriol. 172:6026-6034(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A HEAT SHOCK PROTEIN.
    6. "A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli."
      Arribas J., Castano J.G.
      J. Biol. Chem. 268:21165-21171(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli."
      Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.
      Biochem. Biophys. Res. Commun. 203:798-804(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, OPERON.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine."
      Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.
      Cell 114:511-520(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation."
      Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.
      Genes Dev. 18:2292-2301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE.
    11. "Two programmed cell death systems in Escherichia coli: an apoptotic-like death is inhibited by the mazEF-mediated death pathway."
      Erental A., Sharon I., Engelberg-Kulka H.
      PLoS Biol. 10:E1001281-E1001281(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    12. "MazF-induced growth inhibition and persister generation in Escherichia coli."
      Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.
      J. Biol. Chem. 289:4191-4205(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF ANTITOXIN MAZE, DISRUPTION PHENOTYPE.
      Strain: K12 / BW25113 and K12 / MC4100 / ATCC 35695 / DSM 6574.
    13. "Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome."
      Shin D.H., Lee C.S., Chung C.H., Suh S.W.
      J. Mol. Biol. 262:71-76(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    14. "The structure of ClpP at 2.3-A resolution suggests a model for ATP-dependent proteolysis."
      Wang J., Hartling J.A., Flanagan J.M.
      Cell 91:447-456(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 15-207, SUBUNIT.
    15. "The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes."
      Bewley M.C., Graziano V., Griffin K., Flanagan J.M.
      J. Struct. Biol. 153:113-128(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF VAL-17; PRO-18; MET-19; VAL-20; ILE-21; THR-24; GLY-27; ASP-32; ILE-33; TYR-34; PHE-126 AND ASP-185.
    16. "Crystal structure at 1.9 A of E. coli ClpP with a peptide covalently bound at the active site."
      Szyk A., Maurizi M.R.
      J. Struct. Biol. 156:165-174(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207 BOUND TO INHIBITOR, ENZYME REGULATION, SUBUNIT.
    17. "Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP."
      Li D.H., Chung Y.S., Gloyd M., Joseph E., Ghirlando R., Wright G.D., Cheng Y.Q., Maurizi M.R., Guarne A., Ortega J.
      Chem. Biol. 17:959-969(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ANTIBIOTIC, SUBUNIT.
    18. "Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations."
      Kimber M.S., Yu A.Y., Borg M., Leung E., Chan H.S., Houry W.A.
      Structure 18:798-808(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiCLPP_ECOLI
    AccessioniPrimary (citable) accession number: P0A6G7
    Secondary accession number(s): P19245, Q2MBY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: July 22, 2015
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.