CSE2_THET8
ID CSE2_THET8 Reviewed; 169 AA.
AC Q53VY0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=CRISPR-associated protein Cse2;
DE AltName: Full=CRISPR type I-E/ECOLI-associated protein CasB/Cse2;
GN Name=cse2; OrderedLocusNames=TTHB189;
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 (1.80 ANGSTROMS).
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=18798563; DOI=10.1002/prot.22224;
RA Agari Y., Yokoyama S., Kuramitsu S., Shinkai A.;
RT "X-ray crystal structure of a CRISPR-associated protein, Cse2, from Thermus
RT thermophilus HB8.";
RL Proteins 73:1063-1067(2008).
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 -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated CasB/Cse2 family.
CC {ECO:0000305}.
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DR EMBL; AP008227; BAD71985.1; -; Genomic_DNA.
DR RefSeq; WP_011229115.1; NC_006462.1.
DR RefSeq; YP_145428.1; NC_006462.1.
DR PDB; 2ZCA; X-ray; 1.80 A; A/B=1-169.
DR PDB; 4H7A; X-ray; 2.60 A; A/B=1-156.
DR PDBsum; 2ZCA; -.
DR PDBsum; 4H7A; -.
DR AlphaFoldDB; Q53VY0; -.
DR SMR; Q53VY0; -.
DR MINT; Q53VY0; -.
DR EnsemblBacteria; BAD71985; BAD71985; BAD71985.
DR GeneID; 3167892; -.
DR KEGG; ttj:TTHB189; -.
DR PATRIC; fig|300852.9.peg.2140; -.
DR HOGENOM; CLU_081588_3_0_0; -.
DR OMA; WARAFYR; -.
DR EvolutionaryTrace; Q53VY0; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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; Plasmid; Reference proteome.
FT CHAIN 1..169
FT /note="CRISPR-associated protein Cse2"
FT /id="PRO_0000418433"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:2ZCA"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2ZCA"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2ZCA"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2ZCA"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:2ZCA"
SQ SEQUENCE 169 AA; 19405 MW; FC9C4C109071B71B CRC64;
MSPGERFLDW LKRLQGQKAW TAARAAFRRS LAFPPGAYPR AMPYVEPFLA KGDWRQEERE
AHYLVAALYA LKDGDHQVGR TLARALWEKA QGSASVEKRF LALLEADRDQ IAFRLRQAVA
LVEGGIDFAR LLDDLLRWFS PERHVQARWA REYYGAGASE EEKKKEVEA