CSA5B_SACS2
ID CSA5B_SACS2 Reviewed; 150 AA.
AC Q97Y90;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=CRISPR type I-A cluster 2/Apern-associated protein Csa5-2;
DE AltName: Full=Probable CRISPR toxin Csa5 {ECO:0000303|PubMed:25277654};
GN Name=csa5; OrderedLocusNames=SSO1443;
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 SUBUNIT.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=21507944; DOI=10.1074/jbc.m111.238485;
RA Lintner N.G., Kerou M., Brumfield S.K., Graham S., Liu H., Naismith J.H.,
RA Sdano M., Peng N., She Q., Copie V., Young M.J., White M.F., Lawrence C.M.;
RT "Structural and functional characterization of an archaeal clustered
RT regularly interspaced short palindromic repeat (CRISPR)-associated complex
RT for antiviral defense (CASCADE).";
RL J. Biol. Chem. 286:21643-21656(2011).
RN [3]
RP SUBUNIT, AND MUTAGENESIS OF ASP-32.
RX PubMed=23846216; DOI=10.4161/rna.23854;
RA Reeks J., Graham S., Anderson L., Liu H., White M.F., Naismith J.H.;
RT "Structure of the archaeal Cascade subunit Csa5: relating the small
RT subunits of CRISPR effector complexes.";
RL RNA Biol. 10:762-769(2013).
RN [4]
RP FUNCTION AS A TOXIN, SUBUNIT, AND MUTAGENESIS OF ASP-32.
RC STRAIN=P2 / 5E6;
RX PubMed=25277654; DOI=10.1016/j.jmb.2014.09.016;
RA He F., Chen L., Peng X.;
RT "First experimental evidence for the presence of a CRISPR toxin in
RT sulfolobus.";
RL J. Mol. Biol. 426:3683-3688(2014).
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 {ECO:0000305}.
CC -!- FUNCTION: In strain P2 toxic when expressed in vivo in the absence of
CC CRISPR loci A-D (strain P2 contains 6 CRISPR loci in all). It causes
CC strong growth inhibition, a significant proportion of cells have
CC degraded or no DNA by 20-24 post-induction (PubMed:25277654).
CC {ECO:0000269|PubMed:25277654}.
CC -!- SUBUNIT: Probably oligomeric upon overexpression; does not interact
CC with a Cas5 (Sso1441)/Cas7 (Sso1442)/crRNA complex (PubMed:23846216).
CC Forms dimer and tetramer-sized oligomers when overexpressed in the
CC absence of CRISPR loci A-D; the oligomers are probably responsible for
CC its toxicity in the absence of CRISPR loci A-D (PubMed:25277654). Part
CC of the aCascade ribonucleoprotein complex, minimally composed of Cas7
CC (formerly Csa2) and Cas5a, which binds crRNA. Other possible components
CC of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while
CC SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly
CC associated. Csa2 is probably the major RNA-binding subunit. The Csa2-
CC Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably
CC forming an R-loop. Purified aCascade forms a filament about 6 nm in
CC width (PubMed:21507944). {ECO:0000269|PubMed:21507944,
CC ECO:0000269|PubMed:23846216, ECO:0000269|PubMed:25277654}.
CC -!- MISCELLANEOUS: The aCascade complex was purified from strain P1.
CC {ECO:0000269|PubMed:21507944}.
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DR EMBL; AE006641; AAK41676.1; -; Genomic_DNA.
DR PIR; E90302; E90302.
DR RefSeq; WP_010923408.1; NC_002754.1.
DR AlphaFoldDB; Q97Y90; -.
DR STRING; 273057.SSO1443; -.
DR EnsemblBacteria; AAK41676; AAK41676; SSO1443.
DR GeneID; 27427811; -.
DR KEGG; sso:SSO1443; -.
DR PATRIC; fig|273057.12.peg.1472; -.
DR eggNOG; arCOG03823; Archaea.
DR HOGENOM; CLU_1811533_0_0_2; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR010157; CRISPR-assoc_Cas5.
DR Pfam; PF09702; Cas_Csa5; 1.
DR TIGRFAMs; TIGR01878; cas_Csa5; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Reference proteome; Toxin.
FT CHAIN 1..150
FT /note="CRISPR type I-A cluster 2/Apern-associated protein
FT Csa5-2"
FT /id="PRO_0000417888"
FT MUTAGEN 32
FT /note="D->A: In strain P2 protein is soluble upon
FT overexpression, behaves as a monomer. No longer toxic when
FT expressed in vivo in the absence of CRISPR loci A-D."
FT /evidence="ECO:0000269|PubMed:23846216,
FT ECO:0000269|PubMed:25277654"
SQ SEQUENCE 150 AA; 16487 MW; 50D18F528A157F1B CRC64;
MAQKSEKENI IGRIANLLAV GFLYSESPTL VDRFANALSK EAVTKVLYDV QRIVQMGIDR
SEIATTTITI QGKDYPAQGK DYPAVNVNSS GAKYTVVGYL PTSQDIEDFL RMIEEDVYYA
RKAGALAMSI ANRIKLGSKQ SKSEQGGEKK
