CSN2_ENTFL
ID CSN2_ENTFL Reviewed; 219 AA.
AC C7UDU4;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=CRISPR-associated protein Csn2;
GN Name=csn2; ORFNames=EFDG_01320;
OS Enterococcus faecalis (Streptococcus faecalis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 4200;
RG The Broad Institute Genome Sequencing Platform;
RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The genome sequence of Enterococcus faecalis strain ATCC 4200.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH CALCIUM, SUBUNIT,
RP AND DNA-BINDING.
RC STRAIN=ATCC 4200;
RX PubMed=21697083; DOI=10.1074/jbc.m111.256263;
RA Nam K.H., Kurinov I., Ke A.;
RT "Crystal structure of clustered regularly interspaced short palindromic
RT repeats (CRISPR)-associated Csn2 protein revealed Ca2+-dependent double-
RT stranded DNA binding activity.";
RL J. Biol. Chem. 286:30759-30768(2011).
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21697083}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csn2 protein family.
CC {ECO:0000305}.
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DR EMBL; GG670377; EEU16261.1; -; Genomic_DNA.
DR PDB; 3S5U; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-219.
DR PDBsum; 3S5U; -.
DR AlphaFoldDB; C7UDU4; -.
DR SMR; C7UDU4; -.
DR HOGENOM; CLU_109392_0_0_9; -.
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.
FT CHAIN 1..219
FT /note="CRISPR-associated protein Csn2"
FT /id="PRO_0000418341"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21697083"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:21697083"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3S5U"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3S5U"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3S5U"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3S5U"
SQ SEQUENCE 219 AA; 25407 MW; 805E67157A12B6D3 CRC64;
MRVNFSLLEE PIEIEKATFL TIKDVQSFAH LVKLIYQYDG ENELKLFDAQ QKGLKPTELF
VVTDILGYDV NSAATLKLIY GDLEAQLNDK PEVKSMIEKL TGTISQLIGY ELLEHEMDLE
EDGIIVQELF KALGIKIETT SDTIFEKVME ITQVHRYLSK KKLLIFINAC TYLTEDEVQQ
VVEYISLNNV DVLFLEQRVV QNRFQYILDE NFYLSYEKA
