CAS6_ECOLI
ID CAS6_ECOLI Reviewed; 199 AA.
AC Q46897; Q2MA73;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=CRISPR system Cascade subunit CasE;
DE EC=3.1.-.-;
DE AltName: Full=CasE endoRNase;
DE AltName: Full=crRNA endonuclease;
GN Name=casE; Synonyms=cas6e, ygcH; OrderedLocusNames=b2756, JW2726;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION AS AN ENDORIBONUCLEASE, SUBUNIT, COFACTOR, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-20.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18703739; DOI=10.1126/science.1159689;
RA Brouns S.J., Jore M.M., Lundgren M., Westra E.R., Slijkhuis R.J.,
RA Snijders A.P., Dickman M.J., Makarova K.S., Koonin E.V., van der Oost J.;
RT "Small CRISPR RNAs guide antiviral defense in prokaryotes.";
RL Science 321:960-964(2008).
RN [4]
RP OPERON STRUCTURE, AND INDUCTION BY LEUO.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
RN [5]
RP INDUCTION BY H-NS.
RC STRAIN=K12;
RX PubMed=20132443; DOI=10.1111/j.1365-2958.2010.07073.x;
RA Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.;
RT "Identification and characterization of E. coli CRISPR-cas promoters and
RT their silencing by H-NS.";
RL Mol. Microbiol. 75:1495-1512(2010).
RN [6]
RP FUNCTION AS AN INHIBITOR OF YGBT (CAS1), AND INTERACTION WITH YGBT.
RC STRAIN=K12;
RX PubMed=21219465; DOI=10.1111/j.1365-2958.2010.07465.x;
RA Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B.,
RA Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S.,
RA Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J.,
RA Edwards A.M., Yakunin A.F.;
RT "A dual function of the CRISPR-Cas system in bacterial antivirus immunity
RT and DNA repair.";
RL Mol. Microbiol. 79:484-502(2011).
RN [7]
RP FUNCTION AS AN ENDONUCLEASE, ROLE IN PLASMID SILENCING, SUBUNIT, INDUCTION
RP BY BAER, MUTAGENESIS OF HIS-20, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=21255106; DOI=10.1111/j.1365-2958.2010.07482.x;
RA Perez-Rodriguez R., Haitjema C., Huang Q., Nam K.H., Bernardis S., Ke A.,
RA DeLisa M.P.;
RT "Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in
RT Escherichia coli.";
RL Mol. Microbiol. 79:584-599(2011).
RN [8]
RP FUNCTION IN CASCADE, MASS SPECTROMETRY, SUBUNIT, STRUCTURE BY ELECTRON
RP MICROSCOPY, INTERACTION WITH CASA AND CASC, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=21460843; DOI=10.1038/nsmb.2019;
RA Jore M.M., Lundgren M., van Duijn E., Bultema J.B., Westra E.R.,
RA Waghmare S.P., Wiedenheft B., Pul U., Wurm R., Wagner R., Beijer M.R.,
RA Barendregt A., Zhou K., Snijders A.P., Dickman M.J., Doudna J.A.,
RA Boekema E.J., Heck A.J., van der Oost J., Brouns S.J.;
RT "Structural basis for CRISPR RNA-guided DNA recognition by Cascade.";
RL Nat. Struct. Mol. Biol. 18:529-536(2011).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CASCADE WITH AND WITHOUT TARGET RNA,
RP RNA-BINDING, AND INTERACTION WITH CASB AND CASC.
RC STRAIN=K12;
RX PubMed=21938068; DOI=10.1038/nature10402;
RA Wiedenheft B., Lander G.C., Zhou K., Jore M.M., Brouns S.J.,
RA van der Oost J., Doudna J.A., Nogales E.;
RT "Structures of the RNA-guided surveillance complex from a bacterial immune
RT system.";
RL Nature 477:486-489(2011).
RN [10]
RP FUNCTION IN R-LOOP FORMATION, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21699496; DOI=10.1042/bj20110901;
RA Howard J.A., Delmas S., Ivancic-Bace I., Bolt E.L.;
RT "Helicase dissociation and annealing of RNA-DNA hybrids by Escherichia coli
RT Cas3 protein.";
RL Biochem. J. 439:85-95(2011).
RN [11]
RP SUBUNIT, AND CASCADE DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22521689; DOI=10.1016/j.molcel.2012.03.018;
RA Westra E.R., van Erp P.B., Kunne T., Wong S.P., Staals R.H., Seegers C.L.,
RA Bollen S., Jore M.M., Semenova E., Severinov K., de Vos W.M., Dame R.T.,
RA de Vries R., Brouns S.J., van der Oost J.;
RT "CRISPR immunity relies on the consecutive binding and degradation of
RT negatively supercoiled invader DNA by Cascade and Cas3.";
RL Mol. Cell 46:595-605(2012).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA).
CC -!- FUNCTION: CasE is required to process the pre-crRNA into single repeat-
CC spacer units, with an 8-nt 5'-repeat DNA tag that may help other
CC proteins recognize the crRNA. This subunit alone will cleave pre-crRNA,
CC as will CasCDE or CasCE; cleavage does not require divalent metals or
CC ATP. CasCDE alone is also able to form R-loops. Partially inhibits the
CC cleavage of Holliday junctions by YgbT (Cas1). Yields a 5'-hydroxy
CC group and a 2',3'-cyclic phosphate terminus.
CC -!- FUNCTION: A component of Cascade, which participates in CRISPR
CC interference, the third stage of CRISPR immunity. Cascade binds both
CC crRNA and in a sequence-specific manner negatively supercoiled dsDNA
CC target. This leads to the formation of an R-loop in which the crRNA
CC binds the target DNA, displacing the noncomplementary strand. Cas3 is
CC recruited to Cascade, nicks target DNA and then unwinds and cleaves the
CC target, leading to DNA degradation and invader neutralization.
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000269|PubMed:18703739};
CC -!- SUBUNIT: Part of the Cascade ribonucleoprotein complex, with
CC stoichiometry CasA(1),CasB(2),CasC(6),CasD(1),CasE(1)-crRNA(1).
CC Interacts directly with crRNA, CasA, CasB and CasC. Stable subcomplexes
CC of CasBCDE-crRNA and CasCDE-crRNA also form, both of which are able to
CC bind target dsDNA, and CasCDE is able to form R-loops. CasCDE and CasCE
CC complexes have endonuclease activity. Interacts with YgbT (Cas1).
CC Binding of target ssRNA or dsDNA causes a conformational change in the
CC Cascade complex. {ECO:0000269|PubMed:18703739,
CC ECO:0000269|PubMed:21219465, ECO:0000269|PubMed:21255106,
CC ECO:0000269|PubMed:21460843, ECO:0000269|PubMed:21699496,
CC ECO:0000269|PubMed:21938068, ECO:0000269|PubMed:22521689}.
CC -!- INDUCTION: Repressed by H-NS, activated by LeuO. Activated by the BaeSR
CC two-component regulatory system, possibly due to envelope stress. Part
CC of the casABCDE-ygbT-ygbF operon. {ECO:0000269|PubMed:19429622,
CC ECO:0000269|PubMed:20132443, ECO:0000269|PubMed:21255106}.
CC -!- MASS SPECTROMETRY: Mass=22364.7; Mass_error=1.1; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:21460843};
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to bacteriophage lambda
CC infection, loss of plasmid silencing. Decreased levels of crRNA,
CC increased levels of pre-crRNA, prevents pre-crRNA cleavage.
CC {ECO:0000269|PubMed:18703739, ECO:0000269|PubMed:21255106,
CC ECO:0000269|PubMed:21460843}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC family. Subtype I-E/Ecoli subfamily. {ECO:0000305}.
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DR EMBL; U29579; AAA69266.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75798.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76833.1; -; Genomic_DNA.
DR PIR; H65056; H65056.
DR RefSeq; NP_417236.1; NC_000913.3.
DR RefSeq; WP_000281400.1; NZ_LN832404.1.
DR PDB; 4DZD; X-ray; 2.00 A; A=1-199.
DR PDB; 4QYZ; X-ray; 3.03 A; K=1-199.
DR PDB; 4TVX; X-ray; 3.24 A; A/M=1-199.
DR PDB; 4U7U; X-ray; 3.00 A; D/P=1-199.
DR PDB; 5CD4; X-ray; 3.20 A; A/M=1-199.
DR PDB; 5H9E; X-ray; 3.21 A; K=1-199.
DR PDB; 5H9F; X-ray; 2.45 A; K=1-199.
DR PDBsum; 4DZD; -.
DR PDBsum; 4QYZ; -.
DR PDBsum; 4TVX; -.
DR PDBsum; 4U7U; -.
DR PDBsum; 5CD4; -.
DR PDBsum; 5H9E; -.
DR PDBsum; 5H9F; -.
DR AlphaFoldDB; Q46897; -.
DR SMR; Q46897; -.
DR BioGRID; 4261580; 317.
DR ComplexPortal; CPX-1005; Cascade complex.
DR DIP; DIP-12124N; -.
DR IntAct; Q46897; 5.
DR STRING; 511145.b2756; -.
DR PaxDb; Q46897; -.
DR PRIDE; Q46897; -.
DR EnsemblBacteria; AAC75798; AAC75798; b2756.
DR EnsemblBacteria; BAE76833; BAE76833; BAE76833.
DR GeneID; 947226; -.
DR KEGG; ecj:JW2726; -.
DR KEGG; eco:b2756; -.
DR PATRIC; fig|1411691.4.peg.3982; -.
DR EchoBASE; EB2916; -.
DR eggNOG; ENOG5032RWI; Bacteria.
DR HOGENOM; CLU_080982_0_0_6; -.
DR InParanoid; Q46897; -.
DR OMA; HDVVMDA; -.
DR PhylomeDB; Q46897; -.
DR BioCyc; EcoCyc:G7426-MON; -.
DR BioCyc; MetaCyc:G7426-MON; -.
DR PRO; PR:Q46897; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0099048; P:CRISPR-cas system; IDA:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IMP:EcoCyc.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:EcoCyc.
DR GO; GO:0006396; P:RNA processing; IMP:EcoCyc.
DR InterPro; IPR010179; CRISPR-assoc_prot_Cse3.
DR Pfam; PF08798; CRISPR_assoc; 1.
DR SMART; SM01101; CRISPR_assoc; 1.
DR TIGRFAMs; TIGR01907; casE_Cse3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..199
FT /note="CRISPR system Cascade subunit CasE"
FT /id="PRO_0000169321"
FT MUTAGEN 20
FT /note="H->A: Loss of pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:18703739,
FT ECO:0000269|PubMed:21255106"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4DZD"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4DZD"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4U7U"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4DZD"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4DZD"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4U7U"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:4DZD"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4DZD"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4DZD"
SQ SEQUENCE 199 AA; 22293 MW; 1D5C060DD5FCAFAD CRC64;
MYLSKVIIAR AWSRDLYQLH QGLWHLFPNR PDAARDFLFH VEKRNTPEGC HVLLQSAQMP
VSTAVATVIK TKQVEFQLQV GVPLYFRLRA NPIKTILDNQ KRLDSKGNIK RCRVPLIKEA
EQIAWLQRKL GNAARVEDVH PISERPQYFS GDGKSGKIQT VCFEGVLTIN DAPALIDLVQ
QGIGPAKSMG CGLLSLAPL
