CAS2B_THET2
ID CAS2B_THET2 Reviewed; 90 AA.
AC Q746F4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=CRISPR-associated endonuclease Cas2 2;
DE EC=3.1.-.-;
GN Name=cas2b; OrderedLocusNames=TT_P0101;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=22942283; DOI=10.1074/jbc.m112.382598;
RA Nam K.H., Ding F., Haitjema C., Huang Q., DeLisa M.P., Ke A.;
RT "Double-stranded endonuclease activity in Bacillus halodurans clustered
RT regularly interspaced short palindromic repeats (CRISPR)-associated Cas2
RT protein.";
RL J. Biol. Chem. 287:35943-35952(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).
RA Ihsanawati X., Murayama K., Shirouzu M., Yokoyama S.;
RT "Crystal structure of a hypothetical protein TT1823 from Thermus
RT thermophilus.";
RL Submitted (MAY-2005) to the PDB data bank.
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 Involved in the integration of spacer DNA into the CRISPR cassette (By
CC similarity). Functions as a dsDNA endonuclease and as a weak ssRNase
CC (PubMed:22942283). {ECO:0000255|HAMAP-Rule:MF_01471,
CC ECO:0000269|PubMed:22942283}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01471,
CC ECO:0000269|PubMed:22942283};
CC Note=Divalent cations; Mn(2+) is slightly preferred over Mg(2+).
CC {ECO:0000269|PubMed:22942283};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and at pH 6.0.
CC {ECO:0000269|PubMed:22942283}.
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC {ECO:0000255|HAMAP-Rule:MF_01471}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC protein family. {ECO:0000255|HAMAP-Rule:MF_01471}.
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DR EMBL; AE017222; AAS82431.1; -; Genomic_DNA.
DR RefSeq; WP_011174463.1; NC_005838.1.
DR PDB; 1ZPW; X-ray; 1.64 A; X=1-90.
DR PDBsum; 1ZPW; -.
DR AlphaFoldDB; Q746F4; -.
DR SMR; Q746F4; -.
DR STRING; 262724.TT_P0101; -.
DR EnsemblBacteria; AAS82431; AAS82431; TT_P0101.
DR GeneID; 44146538; -.
DR KEGG; tth:TT_P0101; -.
DR eggNOG; COG1343; Bacteria.
DR HOGENOM; CLU_161124_3_0_0; -.
DR OMA; FYPLSGH; -.
DR OrthoDB; 1951170at2; -.
DR EvolutionaryTrace; Q746F4; -.
DR Proteomes; UP000000592; Plasmid pTT27.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR CDD; cd09725; Cas2_I_II_III; 1.
DR HAMAP; MF_01471; Cas2; 1.
DR InterPro; IPR021127; CRISPR_associated_Cas2.
DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR PANTHER; PTHR34405; PTHR34405; 1.
DR Pfam; PF09827; CRISPR_Cas2; 1.
DR TIGRFAMs; TIGR01573; cas2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Plasmid.
FT CHAIN 1..90
FT /note="CRISPR-associated endonuclease Cas2 2"
FT /id="PRO_0000418431"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01471"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1ZPW"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:1ZPW"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1ZPW"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1ZPW"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:1ZPW"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1ZPW"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1ZPW"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1ZPW"
SQ SEQUENCE 90 AA; 10384 MW; 408DB9DA7ABA55A8 CRC64;
MGKRLYAVAY DIPDDTRRVK LANLLKSYGE RVQLSVFECY LDERLLEDLR RRARRLLDLG
QDALRIYPVA GQVEVLGVGP LPELREVQVL
