CSE1_ECOLI
ID CSE1_ECOLI Reviewed; 502 AA.
AC Q46901; Q2MA69;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CRISPR system Cascade subunit CasA;
DE AltName: Full=CRISPR type I-E/Ecoli-associated protein CasA/Cse1;
DE AltName: Full=CRISPR-associated protein CasA/Cse1;
GN Name=casA; Synonyms=cse1, ygcL; OrderedLocusNames=b2760, JW2730;
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 INDUCTION BY LEUO.
RC STRAIN=K12;
RX PubMed=20659289; DOI=10.1111/j.1365-2958.2010.07315.x;
RA Westra E.R., Pul U., Heidrich N., Jore M.M., Lundgren M., Stratmann T.,
RA Wurm R., Raine A., Mescher M., Van Heereveld L., Mastop M., Wagner E.G.,
RA Schnetz K., Van Der Oost J., Wagner R., Brouns S.J.;
RT "H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12
RT can be relieved by the transcription activator LeuO.";
RL Mol. Microbiol. 77:1380-1393(2010).
RN [7]
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 [8]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CASCADE WITH AND WITHOUT TARGET RNA,
RP RNA-BINDING, AND INTERACTION WITH CASB AND CASD.
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 FUNCTION IN CASCADE, MASS SPECTROMETRY, SUBUNIT, STRUCTURE BY ELECTRON
RP MICROSCOPY, INTERACTION WITH CASE, 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 [10]
RP FUNCTION IN TARGET DNA-BINDING IN PRESENCE OF CASCADE.
RX PubMed=22621933; DOI=10.1074/jbc.c112.379503;
RA Mulepati S., Orr A., Bailey S.;
RT "Crystal structure of the largest subunit of a bacterial RNA-guided immune
RT complex and its role in DNA target binding.";
RL J. Biol. Chem. 287:22445-22449(2012).
RN [11]
RP INTERACTION WITH CAS3, 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).
RN [12]
RP FUNCTION IN TARGET DNA-BINDING IN PRESENCE OF CASCADE, AND MUTAGENESIS OF
RP PHE-129; VAL-130 AND ASN-131.
RC STRAIN=K12;
RX PubMed=22521690; DOI=10.1016/j.molcel.2012.03.020;
RA Sashital D.G., Wiedenheft B., Doudna J.A.;
RT "Mechanism of foreign DNA selection in a bacterial adaptive immune
RT system.";
RL Mol. Cell 46:606-615(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, probably via interactions with CasA, nicks target
CC DNA and then unwinds and cleaves the target, leading to DNA degradation
CC and invader neutralization. CasA is not required for formation of
CC Cascade, but probably enhances binding to and subsequent recognition of
CC both target dsDNA and ssDNA.
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 the 5' end of crRNA, CasB, CasD and CasE.
CC Binding of target ssRNA or dsDNA causes a conformational change in the
CC Cascade complex; CasA is required for high affinity target DNA binding.
CC Interacts with Cas3 once Cascade has recognized target DNA.
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:20659289,
CC ECO:0000269|PubMed:21255106}.
CC -!- MASS SPECTROMETRY: Mass=55972.4; Mass_error=14.8; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:21460843};
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to bacteriophage lambda
CC infection, loss of plasmid silencing. {ECO:0000269|PubMed:18703739,
CC ECO:0000269|PubMed:21255106, ECO:0000269|PubMed:21460843}.
CC -!- SIMILARITY: Belongs to the CRISPR associated protein CasA/Cse1 family.
CC Type I-E/Ecoli subfamily. {ECO:0000305}.
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DR EMBL; U29579; AAA69270.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75802.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76837.1; -; Genomic_DNA.
DR PIR; D65057; D65057.
DR RefSeq; NP_417240.1; NC_000913.3.
DR RefSeq; WP_001050401.1; NZ_LN832404.1.
DR PDB; 4QYZ; X-ray; 3.03 A; A=1-502.
DR PDB; 4TVX; X-ray; 3.24 A; I/U=1-502.
DR PDB; 4U7U; X-ray; 3.00 A; A/M=1-502.
DR PDB; 5CD4; X-ray; 3.20 A; I/U=1-502.
DR PDB; 5H9E; X-ray; 3.21 A; A=1-502.
DR PDB; 5H9F; X-ray; 2.45 A; A=1-502.
DR PDBsum; 4QYZ; -.
DR PDBsum; 4TVX; -.
DR PDBsum; 4U7U; -.
DR PDBsum; 5CD4; -.
DR PDBsum; 5H9E; -.
DR PDBsum; 5H9F; -.
DR AlphaFoldDB; Q46901; -.
DR SMR; Q46901; -.
DR BioGRID; 4260748; 358.
DR BioGRID; 851554; 1.
DR ComplexPortal; CPX-1005; Cascade complex.
DR DIP; DIP-12128N; -.
DR IntAct; Q46901; 8.
DR STRING; 511145.b2760; -.
DR PaxDb; Q46901; -.
DR PRIDE; Q46901; -.
DR EnsemblBacteria; AAC75802; AAC75802; b2760.
DR EnsemblBacteria; BAE76837; BAE76837; BAE76837.
DR GeneID; 947222; -.
DR KEGG; ecj:JW2730; -.
DR KEGG; eco:b2760; -.
DR PATRIC; fig|1411691.4.peg.3978; -.
DR EchoBASE; EB2920; -.
DR eggNOG; ENOG502Z880; Bacteria.
DR HOGENOM; CLU_541555_0_0_6; -.
DR InParanoid; Q46901; -.
DR OMA; FALAYHI; -.
DR BioCyc; EcoCyc:G7430-MON; -.
DR BioCyc; MetaCyc:G7430-MON; -.
DR PRO; PR:Q46901; -.
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:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion 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; cd09669; Cse1_I-E; 1.
DR InterPro; IPR013381; CRISPR-assoc_prot_Cse1.
DR Pfam; PF09481; CRISPR_Cse1; 1.
DR TIGRFAMs; TIGR02547; casA_cse1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; Reference proteome;
KW RNA-binding.
FT CHAIN 1..502
FT /note="CRISPR system Cascade subunit CasA"
FT /id="PRO_0000169324"
FT MUTAGEN 129
FT /note="F->A: 80% increase in phage sensitivity; 500-fold
FT decrease in affinity for target dsDNA."
FT /evidence="ECO:0000269|PubMed:22521690"
FT MUTAGEN 130
FT /note="V->A: 20% increase in phage sensitivity; no change
FT in binding of target dsDNA."
FT /evidence="ECO:0000269|PubMed:22521690"
FT MUTAGEN 131
FT /note="N->A: 45% increase in phage sensitivity; 60-fold
FT decrease in affinity for target dsDNA."
FT /evidence="ECO:0000269|PubMed:22521690"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4U7U"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4U7U"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4U7U"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:5H9F"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:4U7U"
FT HELIX 376..405
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 431..437
FT /evidence="ECO:0007829|PDB:5H9F"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 443..466
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:5H9F"
FT HELIX 476..491
FT /evidence="ECO:0007829|PDB:5H9F"
SQ SEQUENCE 502 AA; 55901 MW; B3ACC755ABE8D965 CRC64;
MNLLIDNWIP VRPRNGGKVQ IINLQSLYCS RDQWRLSLPR DDMELAALAL LVCIGQIIAP
AKDDVEFRHR IMNPLTEDEF QQLIAPWIDM FYLNHAEHPF MQTKGVKAND VTPMEKLLAG
VSGATNCAFV NQPGQGEALC GGCTAIALFN QANQAPGFGG GFKSGLRGGT PVTTFVRGID
LRSTVLLNVL TLPRLQKQFP NESHTENQPT WIKPIKSNES IPASSIGFVR GLFWQPAHIE
LCDPIGIGKC SCCGQESNLR YTGFLKEKFT FTVNGLWPHP HSPCLVTVKK GEVEEKFLAF
TTSAPSWTQI SRVVVDKIIQ NENGNRVAAV VNQFRNIAPQ SPLELIMGGY RNNQASILER
RHDVLMFNQG WQQYGNVINE IVTVGLGYKT ALRKALYTFA EGFKNKDFKG AGVSVHETAE
RHFYRQSELL IPDVLANVNF SQADEVIADL RDKLHQLCEM LFNQSVAPYA HHPKLISTLA
LARATLYKHL RELKPQGGPS NG
