RN393_SACS2
ID RN393_SACS2 Reviewed; 321 AA.
AC Q97YD2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=CRISPR system ring nuclease SSO1393 {ECO:0000303|PubMed:30232454};
DE EC=4.6.1.- {ECO:0000305};
GN OrderedLocusNames=SSO1393;
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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-11 AND LYS-168.
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).
RN [3] {ECO:0007744|PDB:3QYF}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RA Petit P., Xu X., Beloglazova N., Brown G., Savchenko A., Yakunin A.F.;
RT "Crystal structure of the CRISPR-associated protein SSO1393 from Sulfolobus
RT solfataricus.";
RL Submitted (MAR-2011) to the PDB data bank.
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 Slowly degrades cA4 (a tetraadenylate ring) into first a linear
CC tetraadenylate product and secondly into a linear diadenylate product
CC with 5'-OH and 2',3'-cyclic phosphate termini. Is 10-fold less active
CC than SSO2081, suggesting it plays a minor role in cA4 degradation.
CC There may 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 0.024 min(-1). {ECO:0000269|PubMed:30232454};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:30232454, ECO:0000305|Ref.3}.
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; AAK41629.1; -; Genomic_DNA.
DR PIR; F90296; F90296.
DR RefSeq; WP_009990074.1; NC_002754.1.
DR PDB; 3QYF; X-ray; 1.90 A; A/B=1-321.
DR PDBsum; 3QYF; -.
DR AlphaFoldDB; Q97YD2; -.
DR SMR; Q97YD2; -.
DR STRING; 273057.SSO1393; -.
DR EnsemblBacteria; AAK41629; AAK41629; SSO1393.
DR GeneID; 44130249; -.
DR KEGG; sso:SSO1393; -.
DR PATRIC; fig|273057.12.peg.1409; -.
DR eggNOG; arCOG01935; Archaea.
DR HOGENOM; CLU_082641_1_0_2; -.
DR InParanoid; Q97YD2; -.
DR OMA; CAELNTV; -.
DR PhylomeDB; Q97YD2; -.
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; IPR016620; SSO1393.
DR InterPro; IPR013442; SSO1393-like.
DR Pfam; PF09651; Cas_APE2256; 1.
DR PIRSF; PIRSF014470; UCP014470; 1.
DR TIGRFAMs; TIGR02619; TIGR02619; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..321
FT /note="CRISPR system ring nuclease SSO1393"
FT /id="PRO_0000446012"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:30232454"
FT MUTAGEN 11
FT /note="S->A: 32-fold decrease in kcat for degradation of
FT cA4."
FT /evidence="ECO:0000269|PubMed:30232454"
FT MUTAGEN 168
FT /note="K->A: No degradation of cA4."
FT /evidence="ECO:0000269|PubMed:30232454"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3QYF"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:3QYF"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3QYF"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3QYF"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:3QYF"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:3QYF"
SQ SEQUENCE 321 AA; 37448 MW; 4D50669446A9BA64 CRC64;
MEVHVCSVGT SLLKNSLDDD NVRKEIERLG LKDWDRLKFD DDRQNRIKEN FDSLRKMLLK
FIRSKGRRAS AELDSLFSTF EKLKHNKSEI YVFLYSTNTS NSQLAGEVIR DYLIEEGIRS
ELVTVKTISS EENFYEGIVD LFDKVIYRIL KFKEQDNEVY INATPGLKPE SIFLTLAGLL
AGADLIYYKY QEFNDVVILP SPPITIRPKY LDWLIRFAIS GYTLSEKRAE ELGIPVRLLE
AKMLVERKGE DAYRLKDWVR KLLGIYLPIG AQNKYYRVIV EGEGERTFDN EVEAYNYMES
KRKEGKNVRV EVPDRVYFLG L
