CSE1_THET8
ID CSE1_THET8 Reviewed; 502 AA.
AC Q53VY1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=CRISPR-associated protein CasA/Cse1;
DE AltName: Full=CRISPR type I-E/Ecoli-associated protein CasA/Cse1;
GN Name=cse1; Synonyms=casA; OrderedLocusNames=TTHB188;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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) (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Part of the Cascade ribonucleoprotein complex.
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 (By
CC similarity). {ECO:0000250}.
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; AP008227; BAD71984.1; -; Genomic_DNA.
DR RefSeq; WP_011229116.1; NC_006462.1.
DR RefSeq; YP_145427.1; NC_006462.1.
DR PDB; 4AN8; X-ray; 2.30 A; A/B=1-502.
DR PDB; 4EJ3; X-ray; 2.52 A; A/B=1-502.
DR PDB; 4F3E; X-ray; 2.30 A; A/B=1-502.
DR PDBsum; 4AN8; -.
DR PDBsum; 4EJ3; -.
DR PDBsum; 4F3E; -.
DR AlphaFoldDB; Q53VY1; -.
DR SMR; Q53VY1; -.
DR PRIDE; Q53VY1; -.
DR EnsemblBacteria; BAD71984; BAD71984; BAD71984.
DR GeneID; 3167882; -.
DR KEGG; ttj:TTHB188; -.
DR PATRIC; fig|300852.9.peg.2139; -.
DR HOGENOM; CLU_034285_1_0_0; -.
DR OMA; CHTATAP; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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; Plasmid; Reference proteome.
FT CHAIN 1..502
FT /note="CRISPR-associated protein CasA/Cse1"
FT /id="PRO_0000418670"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4AN8"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4F3E"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4F3E"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:4AN8"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:4AN8"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:4AN8"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 368..399
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 425..442
FT /evidence="ECO:0007829|PDB:4AN8"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:4AN8"
FT HELIX 449..472
FT /evidence="ECO:0007829|PDB:4AN8"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4F3E"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:4F3E"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:4AN8"
SQ SEQUENCE 502 AA; 56198 MW; E16782C2AB9CC94B CRC64;
MGSLEKFNLI DEPWIPVLKG GRVVEVGIGE ALLRAHEFAR IETPSPLEEA VLHRLLLAVL
HRALSGPRCP EDVLDWWRKG GFPQDPIRDY LNRFRDRFFL FHPEAPFLQV ADLPEENPLP
WSKLLPELAS GNNPTLFDHT TEENLPKATY AQAARALLVH QAFAPGGLLR RYGVGSAKDA
PVARPALFLP TGQNLLETLL LNLVPYTPED DAPIWEVPPL RLGDLEGART KWPLTGRTRV
YTWPARGVRL LDEGDGVRFM GYGPGVEPLE ATHRDPMVAQ RLDAKGNLLV LRLSEERSFW
RDFSAMLPRQ GGKVAATLEH AENLQGELED EGLEGRITLR VLGQVSDQAK VLDIRREVYP
LPSGLLTPKA EENLEKALKM AEELGQGLKH LAQEVAKAVV GERDRGHGRS PYLEELTKLA
NSLPLERLYW HALDGAFPRF FARVEEEASL DLWREALRGA ALEAWKATRR FLGTGARHLK
ALAQGEQEFG RLLGELGEEV RT
