CSE2_ECOLI
ID CSE2_ECOLI Reviewed; 160 AA.
AC P76632; Q2MA70; Q46900;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CRISPR system Cascade subunit CasB;
GN Name=casB; Synonyms=cse2, ygcK; OrderedLocusNames=b2759, JW2729;
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 SUBUNIT, AND DISRUPTION PHENOTYPE.
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 SUBUNIT, INDUCTION BY BAER, ROLE IN PLASMID SILENCING, AND DISRUPTION
RP 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 [7]
RP FUNCTION IN CASCADE, MASS SPECTROMETRY, SUBUNIT, STRUCTURE BY ELECTRON
RP MICROSCOPY, INTERACTION WITH 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 [8]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CASCADE WITH AND WITHOUT TARGET RNA,
RP RNA-BINDING, AND INTERACTION WITH CASA; CASC AND CASE.
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 [9]
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: 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 -!- SUBUNIT: Homodimer. Part of the Cascade ribonucleoprotein complex, with
CC stoichiometry CasA(1),CasB(2), CasC(6),CasD(1),CasE(1)-crRNA(1). The
CC CasB homodimer forms a cleft that cradles the 3' end of the crRNA.
CC Interacts directly with crRNA, CasA, CasC and CasE. Stable subcomplexes
CC of CasBCDE-crRNA and CasCDE-crRNA also form, both of which are able to
CC bind target dsDNA. Binding of target ssRNA or dsDNA causes a
CC conformational change in the Cascade complex.
CC {ECO:0000269|PubMed:18703739, ECO:0000269|PubMed:21255106,
CC ECO:0000269|PubMed:21460843, ECO:0000269|PubMed:21938068,
CC 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=21261.5; 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. Increased levels of 57 nucleotide
CC crRNA and also 2 and 3 spacer-repeat units.
CC {ECO:0000269|PubMed:18703739, ECO:0000269|PubMed:21255106,
CC ECO:0000269|PubMed:21460843}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated CasB/Cse2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69269.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U29579; AAA69269.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75801.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76836.1; -; Genomic_DNA.
DR PIR; C65057; C65057.
DR RefSeq; NP_417239.1; NC_000913.3.
DR RefSeq; WP_000752800.1; NZ_LN832404.1.
DR PDB; 4QYZ; X-ray; 3.03 A; B/C=1-160.
DR PDB; 4TVX; X-ray; 3.24 A; J/K/V/W=1-160.
DR PDB; 4U7U; X-ray; 3.00 A; B/C/N/O=1-160.
DR PDB; 5CD4; X-ray; 3.20 A; J/K/V/W=1-160.
DR PDB; 5H9E; X-ray; 3.21 A; B/C=1-160.
DR PDB; 5H9F; X-ray; 2.45 A; B/C=1-160.
DR PDBsum; 4QYZ; -.
DR PDBsum; 4TVX; -.
DR PDBsum; 4U7U; -.
DR PDBsum; 5CD4; -.
DR PDBsum; 5H9E; -.
DR PDBsum; 5H9F; -.
DR AlphaFoldDB; P76632; -.
DR SMR; P76632; -.
DR BioGRID; 4260739; 180.
DR ComplexPortal; CPX-1005; Cascade complex.
DR DIP; DIP-12127N; -.
DR IntAct; P76632; 13.
DR STRING; 511145.b2759; -.
DR PaxDb; P76632; -.
DR PRIDE; P76632; -.
DR EnsemblBacteria; AAC75801; AAC75801; b2759.
DR EnsemblBacteria; BAE76836; BAE76836; BAE76836.
DR GeneID; 947223; -.
DR KEGG; ecj:JW2729; -.
DR KEGG; eco:b2759; -.
DR PATRIC; fig|1411691.4.peg.3979; -.
DR EchoBASE; EB2919; -.
DR eggNOG; ENOG5032TS5; Bacteria.
DR HOGENOM; CLU_144604_0_0_6; -.
DR InParanoid; P76632; -.
DR OMA; YQNWSEL; -.
DR BioCyc; EcoCyc:G7429-MON; -.
DR BioCyc; MetaCyc:G7429-MON; -.
DR PRO; PR:P76632; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003676; F:nucleic acid binding; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0099048; P:CRISPR-cas system; IDA:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IMP:EcoCyc.
DR CDD; cd09670; Cse2_I-E; 1.
DR Gene3D; 1.10.520.40; -; 1.
DR InterPro; IPR013382; CRISPR-assoc_prot_Cse2.
DR InterPro; IPR038287; Cse2_sf.
DR Pfam; PF09485; CRISPR_Cse2; 1.
DR TIGRFAMs; TIGR02548; casB_cse2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Reference proteome; RNA-binding.
FT CHAIN 1..160
FT /note="CRISPR system Cascade subunit CasB"
FT /id="PRO_0000169323"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4U7U"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:5H9F"
SQ SEQUENCE 160 AA; 18702 MW; F2493AAD46595E5C CRC64;
MADEIDAMAL YRAWQQLDNG SCAQIRRVSE PDELRDIPAF YRLVQPFGWE NPRHQQALLR
MVFCLSAGKN VIRHQDKKSE QTTGISLGRA LANSGRINER RIFQLIRADR TADMVQLRRL
LTHAEPVLDW PLMARMLTWW GKRERQQLLE DFVLTTNKNA
