CAS2_ALKHC
ID CAS2_ALKHC Reviewed; 96 AA.
AC Q9KFX8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=CRISPR-associated endonuclease Cas2;
DE EC=3.1.-.-;
GN Name=cas2; OrderedLocusNames=BH0342;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.10
RP ANGSTROMS), AND MUTAGENESIS OF ASP-8.
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
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).
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-specific endonuclease, acting on
CC circular and linear DNA; has no activity on ssRNA or ssDNA.
CC {ECO:0000250, ECO:0000269|PubMed:22942283}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22942283};
CC Note=Binds 1 Mg(2+) per homodimer, shared between the Asp-8 pair;
CC divalent cations support activity in decreasing order, Mg(2+) >> Mn(2+)
CC > Fe(2+) > Ni(2+) > Ca(2+). {ECO:0000269|PubMed:22942283};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and Zn(2+). Activated by high
CC concentrations of monovalent cation with a preference for K(+) over
CC Na(+). {ECO:0000269|PubMed:22942283}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-10. {ECO:0000269|PubMed:22942283};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC protein family. {ECO:0000305}.
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DR EMBL; BA000004; BAB04061.1; -; Genomic_DNA.
DR PIR; F83692; F83692.
DR RefSeq; WP_010896523.1; NC_002570.2.
DR PDB; 4ES1; X-ray; 1.10 A; A=1-96.
DR PDB; 4ES2; X-ray; 1.30 A; A=1-96.
DR PDB; 4ES3; X-ray; 1.70 A; A=1-96.
DR PDBsum; 4ES1; -.
DR PDBsum; 4ES2; -.
DR PDBsum; 4ES3; -.
DR AlphaFoldDB; Q9KFX8; -.
DR SMR; Q9KFX8; -.
DR STRING; 272558.10172955; -.
DR EnsemblBacteria; BAB04061; BAB04061; BAB04061.
DR KEGG; bha:BH0342; -.
DR eggNOG; COG1343; Bacteria.
DR HOGENOM; CLU_161124_3_1_9; -.
DR OMA; SVFECEV; -.
DR OrthoDB; 1951170at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 PIRSF; PIRSF032582; 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; Reference proteome.
FT CHAIN 1..96
FT /note="CRISPR-associated endonuclease Cas2"
FT /id="PRO_0000422085"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 8
FT /note="D->N: Loss of dsDNase activity."
FT /evidence="ECO:0000269|PubMed:22942283"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:4ES1"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:4ES1"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4ES1"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4ES1"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:4ES1"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4ES1"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:4ES1"
SQ SEQUENCE 96 AA; 10881 MW; F669C89EBBFB9CBE CRC64;
MLVLITYDVQ TSSMGGTKRL RKVAKACQNY GQRVQNSVFE CIVDSTQLTS LKLELTSLID
EEKDSLRIYR LGNNYKTKVE HIGAKPSIDL EDPLIF
