CSN2_STRP1
ID CSN2_STRP1 Reviewed; 220 AA.
AC Q99ZV9; Q48Z28;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=CRISPR-associated protein Csn2;
GN Name=csn2; OrderedLocusNames=M5005_Spy0772, SPy_1049;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM, SUBUNIT,
RP DNA-BINDING, AND COFACTOR.
RX PubMed=22479393; DOI=10.1371/journal.pone.0033401;
RA Koo Y., Jung D.K., Bae E.;
RT "Crystal structure of Streptococcus pyogenes Csn2 reveals calcium-dependent
RT conformational changes in its tertiary and quaternary structure.";
RL PLoS ONE 7:E33401-E33401(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). Binds dsDNA, binding is disrupted by EGTA. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22479393};
CC Note=Binds up to 2 Ca(2+) per subunit. {ECO:0000269|PubMed:22479393};
CC -!- SUBUNIT: Homotetramer. Binds dsDNA. {ECO:0000269|PubMed:22479393}.
CC -!- INTERACTION:
CC Q99ZV9; Q99ZW1: cas1; NbExp=5; IntAct=EBI-16146316, EBI-16146333;
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csn2 protein family.
CC {ECO:0000305}.
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DR EMBL; AE004092; AAK33939.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51390.1; -; Genomic_DNA.
DR RefSeq; NP_269218.1; NC_002737.2.
DR PDB; 3TOC; X-ray; 2.20 A; A/B=1-220.
DR PDB; 3V7F; X-ray; 2.90 A; A/B=1-220.
DR PDBsum; 3TOC; -.
DR PDBsum; 3V7F; -.
DR AlphaFoldDB; Q99ZV9; -.
DR SMR; Q99ZV9; -.
DR DIP; DIP-61505N; -.
DR IntAct; Q99ZV9; 3.
DR STRING; 1314.HKU360_00837; -.
DR PaxDb; Q99ZV9; -.
DR EnsemblBacteria; AAK33939; AAK33939; SPy_1049.
DR KEGG; spy:SPy_1049; -.
DR KEGG; spz:M5005_Spy0772; -.
DR PATRIC; fig|160490.10.peg.905; -.
DR HOGENOM; CLU_109392_0_0_9; -.
DR OMA; CYQYEED; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11940; -; 2.
DR InterPro; IPR010146; CRISPR-assoc_prot_Csn2-typ.
DR InterPro; IPR038600; Csn2_sf.
DR Pfam; PF09711; Cas_Csn2; 1.
DR TIGRFAMs; TIGR01866; cas_Csn2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Calcium; DNA-binding; Metal-binding;
KW Reference proteome.
FT CHAIN 1..220
FT /note="CRISPR-associated protein Csn2"
FT /id="PRO_0000418343"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22479393"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22479393"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3TOC"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3TOC"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3TOC"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3TOC"
SQ SEQUENCE 220 AA; 25587 MW; 597985229CEC4C5E CRC64;
MNLNFSLLDE PIPLRGGTIL VLEDVCVFSK IVQYCYQYEE DSELKFFDHK MKTIKESEIM
LVTDILGFDV NSSTILKLIH ADLESQFNEK PEVKSMIDKL VATITELIVF ECLENELDLE
YDEITILELI KSLGVKVETQ SDTIFEKCLE ILQIFKYLTK KKLLIFVNSG AFLTKDEVAS
LQEYISLTNL TVLFLEPREL YDFPQYILDE DYFLITKNMV
