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Protein

CRISPR system Cascade subunit CasE

Gene

casE

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

Functioni

CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
CasE is required to process the pre-crRNA into single repeat-spacer units, with an 8-nt 5'-repeat DNA tag that may help other proteins recognize the crRNA. This subunit alone will cleave pre-crRNA, as will CasCDE or CasCE; cleavage does not require divalent metals or ATP. CasCDE alone is also able to form R-loops. Partially inhibits the cleavage of Holliday junctions by YgbT (Cas1). Yields a 5'-hydroxy group and a 2',3'-cyclic phosphate terminus.
A component of Cascade, which participates in CRISPR interference, the third stage of CRISPR immunity. Cascade binds both crRNA and in a sequence-specific manner negatively supercoiled dsDNA target. This leads to the formation of an R-loop in which the crRNA binds the target DNA, displacing the noncomplementary strand. Cas3 is recruited to Cascade, nicks target DNA and then unwinds and cleaves the target, leading to DNA degradation and invader neutralization.

Cofactori

Note: Does not require a metal cofactor.1 Publication

GO - Molecular functioni

  • endoribonuclease activity Source: EcoCyc
  • RNA binding Source: EcoCyc

GO - Biological processi

  • defense response to virus Source: EcoCyc
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: EcoCyc
  • RNA processing Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7426-MONOMER.
ECOL316407:JW2726-MONOMER.
MetaCyc:G7426-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CRISPR system Cascade subunit CasE (EC:3.1.-.-)
Alternative name(s):
CasE endoRNase
crRNA endonuclease
Gene namesi
Name:casE
Synonyms:cas6e, ygcH
Ordered Locus Names:b2756, JW2726
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13115. casE.

Subcellular locationi

GO - Cellular componenti

  • protein complex Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Loss of resistance to bacteriophage lambda infection, loss of plasmid silencing. Decreased levels of crRNA, increased levels of pre-crRNA, prevents pre-crRNA cleavage.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201H → A: Loss of pre-crRNA cleavage. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 199198CRISPR system Cascade subunit CasEPRO_0000169321Add
BLAST

Proteomic databases

PaxDbiQ46897.
PRIDEiQ46897.

Expressioni

Inductioni

Repressed by H-NS, activated by LeuO. Activated by the BaeSR two-component regulatory system, possibly due to envelope stress. Part of the casABCDE-ygbT-ygbF operon.3 Publications

Interactioni

Subunit structurei

Part of the Cascade ribonucleoprotein complex, with stoichiometry CasA1,CasB2,CasC6,CasD1,CasE(1)-crRNA1. Interacts directly with crRNA, CasA, CasB and CasC. Stable subcomplexes of CasBCDE-crRNA and CasCDE-crRNA also form, both of which are able to bind target dsDNA, and CasCDE is able to form R-loops. CasCDE and CasCE complexes have endonuclease activity. Interacts with YgbT (Cas1). Binding of target ssRNA or dsDNA causes a conformational change in the Cascade complex.7 Publications

Protein-protein interaction databases

BioGridi4261580. 317 interactions.
DIPiDIP-12124N.
IntActiQ46897. 2 interactions.
STRINGi511145.b2756.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi10 – 123Combined sources
Beta strandi13 – 153Combined sources
Helixi16 – 249Combined sources
Beta strandi37 – 4610Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi64 – 7310Combined sources
Beta strandi83 – 908Combined sources
Beta strandi93 – 975Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi111 – 1155Combined sources
Helixi119 – 13012Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 14310Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 17010Combined sources
Helixi172 – 18110Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 1893Combined sources
Beta strandi194 – 1985Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DZDX-ray2.00A1-199[»]
4QYZX-ray3.03K1-199[»]
4TVXX-ray3.24A/M1-199[»]
4U7UX-ray3.00D/P1-199[»]
5CD4X-ray3.20A/M1-199[»]
5H9EX-ray3.21K1-199[»]
5H9FX-ray2.45K1-199[»]
ProteinModelPortaliQ46897.
SMRiQ46897. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108Y7V. Bacteria.
ENOG410ZWC5. LUCA.
HOGENOMiHOG000015851.
InParanoidiQ46897.
KOiK19126.
OMAiIGRKKHA.
OrthoDBiEOG6Z6FX3.

Family and domain databases

InterProiIPR010179. CRISPR-assoc_prot_Cse3.
[Graphical view]
PfamiPF08798. CRISPR_assoc. 1 hit.
[Graphical view]
SMARTiSM01101. CRISPR_assoc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01907. casE_Cse3. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q46897-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLSKVIIAR AWSRDLYQLH QGLWHLFPNR PDAARDFLFH VEKRNTPEGC
60 70 80 90 100
HVLLQSAQMP VSTAVATVIK TKQVEFQLQV GVPLYFRLRA NPIKTILDNQ
110 120 130 140 150
KRLDSKGNIK RCRVPLIKEA EQIAWLQRKL GNAARVEDVH PISERPQYFS
160 170 180 190
GDGKSGKIQT VCFEGVLTIN DAPALIDLVQ QGIGPAKSMG CGLLSLAPL
Length:199
Mass (Da):22,293
Last modified:November 1, 1996 - v1
Checksum:i1D5C060DD5FCAFAD
GO

Mass spectrometryi

Molecular mass is 22364.7±1.1 Da from positions 2 - 199. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29579 Genomic DNA. Translation: AAA69266.1.
U00096 Genomic DNA. Translation: AAC75798.1.
AP009048 Genomic DNA. Translation: BAE76833.1.
PIRiH65056.
RefSeqiNP_417236.1. NC_000913.3.
WP_000281400.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75798; AAC75798; b2756.
BAE76833; BAE76833; BAE76833.
GeneIDi947226.
KEGGiecj:JW2726.
eco:b2756.
PATRICi32120922. VBIEscCol129921_2853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29579 Genomic DNA. Translation: AAA69266.1.
U00096 Genomic DNA. Translation: AAC75798.1.
AP009048 Genomic DNA. Translation: BAE76833.1.
PIRiH65056.
RefSeqiNP_417236.1. NC_000913.3.
WP_000281400.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DZDX-ray2.00A1-199[»]
4QYZX-ray3.03K1-199[»]
4TVXX-ray3.24A/M1-199[»]
4U7UX-ray3.00D/P1-199[»]
5CD4X-ray3.20A/M1-199[»]
5H9EX-ray3.21K1-199[»]
5H9FX-ray2.45K1-199[»]
ProteinModelPortaliQ46897.
SMRiQ46897. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261580. 317 interactions.
DIPiDIP-12124N.
IntActiQ46897. 2 interactions.
STRINGi511145.b2756.

Proteomic databases

PaxDbiQ46897.
PRIDEiQ46897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75798; AAC75798; b2756.
BAE76833; BAE76833; BAE76833.
GeneIDi947226.
KEGGiecj:JW2726.
eco:b2756.
PATRICi32120922. VBIEscCol129921_2853.

Organism-specific databases

EchoBASEiEB2916.
EcoGeneiEG13115. casE.

Phylogenomic databases

eggNOGiENOG4108Y7V. Bacteria.
ENOG410ZWC5. LUCA.
HOGENOMiHOG000015851.
InParanoidiQ46897.
KOiK19126.
OMAiIGRKKHA.
OrthoDBiEOG6Z6FX3.

Enzyme and pathway databases

BioCyciEcoCyc:G7426-MONOMER.
ECOL316407:JW2726-MONOMER.
MetaCyc:G7426-MONOMER.

Miscellaneous databases

PROiQ46897.

Family and domain databases

InterProiIPR010179. CRISPR-assoc_prot_Cse3.
[Graphical view]
PfamiPF08798. CRISPR_assoc. 1 hit.
[Graphical view]
SMARTiSM01101. CRISPR_assoc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01907. casE_Cse3. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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.
  3. Cited for: FUNCTION AS AN ENDORIBONUCLEASE, SUBUNIT, COFACTOR, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-20.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Involvement of the leucine response transcription factor LeuO in regulation of the genes for sulfa drug efflux."
    Shimada T., Yamamoto K., Ishihama A.
    J. Bacteriol. 191:4562-4571(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: OPERON STRUCTURE, INDUCTION BY LEUO.
    Strain: K12 / BW25113.
  5. "Identification and characterization of E. coli CRISPR-cas promoters and their silencing by H-NS."
    Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.
    Mol. Microbiol. 75:1495-1512(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY H-NS.
    Strain: K12.
  6. Cited for: FUNCTION AS AN INHIBITOR OF YGBT (CAS1), INTERACTION WITH YGBT.
    Strain: K12.
  7. "Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in Escherichia coli."
    Perez-Rodriguez R., Haitjema C., Huang Q., Nam K.H., Bernardis S., Ke A., DeLisa M.P.
    Mol. Microbiol. 79:584-599(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ENDONUCLEASE, ROLE IN PLASMID SILENCING, SUBUNIT, INDUCTION BY BAER, MUTAGENESIS OF HIS-20, DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  8. Cited for: FUNCTION IN CASCADE, MASS SPECTROMETRY, SUBUNIT, STRUCTURE BY ELECTRON MICROSCOPY, INTERACTION WITH CASA AND CASC, DISRUPTION PHENOTYPE.
    Strain: K12.
  9. "Structures of the RNA-guided surveillance complex from a bacterial immune system."
    Wiedenheft B., Lander G.C., Zhou K., Jore M.M., Brouns S.J., van der Oost J., Doudna J.A., Nogales E.
    Nature 477:486-489(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY OF CASCADE WITH AND WITHOUT TARGET RNA, RNA-BINDING, INTERACTION WITH CASB AND CASC.
    Strain: K12.
  10. "Helicase dissociation and annealing of RNA-DNA hybrids by Escherichia coli Cas3 protein."
    Howard J.A., Delmas S., Ivancic-Bace I., Bolt E.L.
    Biochem. J. 439:85-95(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN R-LOOP FORMATION, SUBUNIT.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "CRISPR immunity relies on the consecutive binding and degradation of negatively supercoiled invader DNA by Cascade and Cas3."
    Westra E.R., van Erp P.B., Kunne T., Wong S.P., Staals R.H., Seegers C.L., Bollen S., Jore M.M., Semenova E., Severinov K., de Vos W.M., Dame R.T., de Vries R., Brouns S.J., van der Oost J.
    Mol. Cell 46:595-605(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, CASCADE DNA-BINDING.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiCAS6_ECOLI
AccessioniPrimary (citable) accession number: Q46897
Secondary accession number(s): Q2MA73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.