RN081_SACS2
ID RN081_SACS2 Reviewed; 178 AA.
AC Q7LYJ6;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=CRISPR system ring nuclease SSO2081 {ECO:0000303|PubMed:30232454};
DE EC=4.6.1.- {ECO:0000305};
GN OrderedLocusNames=SSO2081;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF SER-11 AND 105-ARG-LYS-106.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=30232454; DOI=10.1038/s41586-018-0557-5;
RA Athukoralage J.S., Rouillon C., Graham S., Grueschow S., White M.F.;
RT "Ring nucleases deactivate type III CRISPR ribonucleases by degrading
RT cyclic oligoadenylate.";
RL Nature 562:277-280(2018).
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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA)
CC (Probable). A nuclease that degrades cyclic oligoadenylates (cOA),
CC second messengers that induce an antiviral state important for defense
CC against invading nucleic acids. Destruction of cOA deactivates the Csx1
CC ribonuclease, preventing uncontrolled degradation of cellular RNA.
CC Degrades cA4 (a tetraadenylate ring) into a linear diadenylate product
CC with 5'-OH and 2',3'-cyclic phosphate termini. Is 10-fold more active
CC than SSO1393, suggesting this is the major cA4 degradation enzyme. Is
CC highly specific for cA4; it has very poor activity on cA6 and no
CC discernible activity against a number of cyclic dinucletides. There may
CC be 2 active sites per homodimer (PubMed:30232454).
CC {ECO:0000269|PubMed:30232454, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclic tetraadenylate = 2 5'-hydroxy-diadenylate 2',3'-cylic
CC phosphate; Xref=Rhea:RHEA:58012, ChEBI:CHEBI:142457,
CC ChEBI:CHEBI:142458; Evidence={ECO:0000269|PubMed:30232454};
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000269|PubMed:30232454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.23 min(-1). {ECO:0000269|PubMed:30232454};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q97YD2,
CC ECO:0000305|PubMed:30232454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:30232454}.
CC -!- SIMILARITY: Belongs to the cOA ring nuclease family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42262.1; -; Genomic_DNA.
DR PIR; S73092; S73092.
DR RefSeq; WP_009989802.1; NC_002754.1.
DR AlphaFoldDB; Q7LYJ6; -.
DR SMR; Q7LYJ6; -.
DR STRING; 273057.SSO2081; -.
DR DNASU; 1453589; -.
DR EnsemblBacteria; AAK42262; AAK42262; SSO2081.
DR GeneID; 44130787; -.
DR KEGG; sso:SSO2081; -.
DR PATRIC; fig|273057.12.peg.2159; -.
DR eggNOG; arCOG03847; Archaea.
DR HOGENOM; CLU_1514679_0_0_2; -.
DR InParanoid; Q7LYJ6; -.
DR OMA; KIMFICC; -.
DR PhylomeDB; Q7LYJ6; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR019092; CRISPR-assoc_prot_NE0113/Csx12.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR Pfam; PF09623; Cas_NE0113; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..178
FT /note="CRISPR system ring nuclease SSO2081"
FT /id="PRO_0000446011"
FT REGION 105..106
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:30232454"
FT MUTAGEN 11
FT /note="S->A: 3.5-fold decrease in kcat for degradation of
FT cA4."
FT /evidence="ECO:0000269|PubMed:30232454"
FT MUTAGEN 105..106
FT /note="RK->AA: No degradation of cA4."
FT /evidence="ECO:0000269|PubMed:30232454"
SQ SEQUENCE 178 AA; 20213 MW; B0078636F21B2A03 CRC64;
MVKLVATLGT SPGGVIESFL YLVKKGENID EVRVVTTSNA EVKKAWRIVR LMFVCCIQEK
FPKVEISEHP LDIEDIYSED DLRKVREFVE KQLGEGDYLD ITGGRKSMSV AAALAAKNKG
VKIITSIIPQ DDYNKISKKV RELKEIPEIK NRGECRQEMK ETYCSLIVQD ARSIEFEI
