CASC_ECOLI
ID CASC_ECOLI Reviewed; 363 AA.
AC Q46899; Q2MA71;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=CRISPR system Cascade subunit CasC;
GN Name=casC; Synonyms=cas4, cse4, ygcJ; OrderedLocusNames=b2758, JW2728;
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 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 INTERACTION WITH CASD AND CASE, SUBUNIT, INDUCTION BY BAER, ROLE IN PLASMID
RP SILENCING, 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; CASB; CASD AND CASE, AND DISRUPTION
RP 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 CASA; CASB; CASD 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 [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: 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. CasCDE
CC alone is also able to form R-loops.
CC -!- SUBUNIT: Part of the Cascade ribonucleoprotein complex, with
CC stoichiometry CasA(1),CasB(2),CasC(6),CasD(1),CasE(1)-crRNA(1). The 6
CC CasC subunits make a helical stack forming a groove in which the crRNA
CC lies. Interacts directly with all of the Cas subunits. Stable
CC subcomplexes of CasBCDE-crRNA and CasCDE-crRNA also form, both of which
CC are able to bind target dsDNA, and at least CasCDE is able to form R-
CC loops. CasCDE and CasCE complexes have endonuclease activity. Interacts
CC with YgbT (Cas1). Binding of target ssRNA or dsDNA causes a
CC conformational change in the Cascade complex.
CC {ECO:0000269|PubMed:18703739, ECO:0000269|PubMed:21219465,
CC ECO:0000269|PubMed:21255106, ECO:0000269|PubMed:21460843,
CC ECO:0000269|PubMed:21699496, 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=39896.3; Mass_error=1.3; 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}.
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DR EMBL; U29579; AAA69268.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75800.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76835.1; -; Genomic_DNA.
DR PIR; B65057; B65057.
DR RefSeq; NP_417238.1; NC_000913.3.
DR RefSeq; WP_000064450.1; NZ_LN832404.1.
DR PDB; 4QYZ; X-ray; 3.03 A; D/E/F/G/H/I=1-363.
DR PDB; 4TVX; X-ray; 3.24 A; B/C/D/E/F/G/N/O/P/Q/R/S=1-363.
DR PDB; 4U7U; X-ray; 3.00 A; E/F/G/H/I/J/Q/R/S/T/U/V=1-363.
DR PDB; 5CD4; X-ray; 3.20 A; B/C/D/E/F/G/N/O/P/Q/R/S=1-363.
DR PDB; 5H9E; X-ray; 3.21 A; D/E/F/G/H/I=1-363.
DR PDB; 5H9F; X-ray; 2.45 A; D/E/F/G/H/I=1-363.
DR PDBsum; 4QYZ; -.
DR PDBsum; 4TVX; -.
DR PDBsum; 4U7U; -.
DR PDBsum; 5CD4; -.
DR PDBsum; 5H9E; -.
DR PDBsum; 5H9F; -.
DR AlphaFoldDB; Q46899; -.
DR SMR; Q46899; -.
DR BioGRID; 4262275; 608.
DR ComplexPortal; CPX-1005; Cascade complex.
DR DIP; DIP-12126N; -.
DR IntAct; Q46899; 4.
DR STRING; 511145.b2758; -.
DR PaxDb; Q46899; -.
DR PRIDE; Q46899; -.
DR EnsemblBacteria; AAC75800; AAC75800; b2758.
DR EnsemblBacteria; BAE76835; BAE76835; BAE76835.
DR GeneID; 947224; -.
DR KEGG; ecj:JW2728; -.
DR KEGG; eco:b2758; -.
DR PATRIC; fig|1411691.4.peg.3980; -.
DR EchoBASE; EB2918; -.
DR eggNOG; COG1857; Bacteria.
DR HOGENOM; CLU_044824_1_0_6; -.
DR InParanoid; Q46899; -.
DR OMA; PTGKQNT; -.
DR PhylomeDB; Q46899; -.
DR BioCyc; EcoCyc:G7428-MON; -.
DR BioCyc; MetaCyc:G7428-MON; -.
DR BRENDA; 3.1.12.1; 2026.
DR PRO; PR:Q46899; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0071667; F:DNA/RNA hybrid binding; 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 CDD; cd09646; Cas7_I-E; 1.
DR InterPro; IPR010148; CRISPR-assoc_prot_CT1975.
DR Pfam; PF09344; Cas_CT1975; 1.
DR TIGRFAMs; TIGR01869; casC_Cse4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..363
FT /note="CRISPR system Cascade subunit CasC"
FT /id="PRO_0000169322"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5H9E"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5CD4"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:5CD4"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:5CD4"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:4U7U"
SQ SEQUENCE 363 AA; 40025 MW; D9A99E0CBBD2B956 CRC64;
MSNFINIHVL ISHSPSCLNR DDMNMQKDAI FGGKRRVRIS SQSLKRAMRK SGYYAQNIGE
SSLRTIHLAQ LRDVLRQKLG ERFDQKIIDK TLALLSGKSV DEAEKISADA VTPWVVGEIA
WFCEQVAKAE ADNLDDKKLL KVLKEDIAAI RVNLQQGVDI ALSGRMATSG MMTELGKVDG
AMSIAHAITT HQVDSDIDWF TAVDDLQEQG SAHLGTQEFS SGVFYRYANI NLAQLQENLG
GASREQALEI ATHVVHMLAT EVPGAKQRTY AAFNPADMVM VNFSDMPLSM ANAFEKAVKA
KDGFLQPSIQ AFNQYWDRVA NGYGLNGAAA QFSLSDVDPI TAQVKQMPTL EQLKSWVRNN
GEA
