CSN2_STRA8
ID CSN2_STRA8 Reviewed; 221 AA.
AC E7S4M0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=CRISPR-associated protein Csn2;
GN Name=csn2; ORFNames=HMPREF9171_1216;
OS Streptococcus agalactiae (strain ATCC 13813 / DSM 2134 / JCM 5671 / NCIMB
OS 701348 / NCTC 8181).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13813 / DSM 2134 / JCM 5671 / NCIMB 701348 / NCTC 8181;
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 3-221, COFACTOR, SUBUNIT,
RP DNA-BINDING, AND MUTAGENESIS OF TYR-29; LYS-132 AND 199-ARG-ARG-200.
RC STRAIN=ATCC 13813 / DSM 2134 / JCM 5671 / NCIMB 701348 / NCTC 8181;
RX PubMed=22531577; DOI=10.1016/j.jsb.2012.04.006;
RA Ellinger P., Arslan Z., Wurm R., Tschapek B., Mackenzie C., Pfeffer K.,
RA Panjikar S., Wagner R., Schmitt L., Gohlke H., Pul U., Smits S.H.;
RT "The crystal structure of the CRISPR-associated protein Csn2 from
RT Streptococcus agalactiae.";
RL J. Struct. Biol. 178:350-362(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:22531577};
CC -!- SUBUNIT: Homodimer, in solution forms homotetramers.
CC {ECO:0000269|PubMed:22531577}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csn2 protein family.
CC {ECO:0000305}.
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DR EMBL; AEQQ01000063; EFV97264.1; -; Genomic_DNA.
DR RefSeq; WP_000590708.1; NZ_GL636070.1.
DR PDB; 3QHQ; X-ray; 2.00 A; A/B=1-221.
DR PDBsum; 3QHQ; -.
DR AlphaFoldDB; E7S4M0; -.
DR SMR; E7S4M0; -.
DR PRIDE; E7S4M0; -.
DR PATRIC; fig|888745.3.peg.1178; -.
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..221
FT /note="CRISPR-associated protein Csn2"
FT /id="PRO_0000418342"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT MUTAGEN 29
FT /note="Y->A,W: Alters binding of dsDNA but does not abolish
FT it."
FT /evidence="ECO:0000269|PubMed:22531577"
FT MUTAGEN 132
FT /note="K->A: Abolishes dsDNA binding."
FT /evidence="ECO:0000269|PubMed:22531577"
FT MUTAGEN 199..200
FT /note="RR->AA: Alters binding of dsDNA but does not abolish
FT it."
FT /evidence="ECO:0000269|PubMed:22531577"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3QHQ"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3QHQ"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3QHQ"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3QHQ"
SQ SEQUENCE 221 AA; 25650 MW; 15CED334AD5530AD CRC64;
MIKINFPILD EPLVLSNATI LTIEDVSVYS SLVKHFYQYD VDEHLKLFDD KQKSLKATEL
MLVTDILGYD VNSAPILKLI HGDLENQFNE KPEVKSMVEK LAATITELIA FECLENELDL
EYDEITILEL IKVLGVKIET QSDTIFEKCF EIIQVYNYLT KKNLLVFVNS GAYLTKDEVI
KLCEYINLMQ KSVLFLEPRR LYDLPQYVID KDYFLIGENM V
