ID   CSM5_STRTR              Reviewed;         357 AA.
AC   A0A0A7HF79;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=CRISPR system Cms protein Csm5;
DE   AltName: Full=CRISPR type III A-associated protein Csm5;
GN   Name=csm5 {ECO:0000303|PubMed:25458845};
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHAGE RESISTANCE, TARGETS
RP   SSRNA, SUBUNIT, AND ANTIVIRAL DEFENSE.
RC   STRAIN=DGCC8004;
RX   PubMed=25458845; DOI=10.1016/j.molcel.2014.09.027;
RA   Tamulaitis G., Kazlauskiene M., Manakova E., Venclovas C., Nwokeoji A.O.,
RA   Dickman M.J., Horvath P., Siksnys V.;
RT   "Programmable RNA shredding by the type III-A CRISPR-Cas system of
RT   Streptococcus thermophilus.";
RL   Mol. Cell 56:506-517(2014).
RN   [2]
RP   SUBUNIT.
RC   STRAIN=DGCC8004;
RX   PubMed=27105119; DOI=10.1016/j.molcel.2016.03.024;
RA   Kazlauskiene M., Tamulaitis G., Kostiuk G., Venclovas C., Siksnys V.;
RT   "Spatiotemporal control of type III-A CRISPR-Cas immunity: coupling DNA
RT   degradation with the target RNA recognition.";
RL   Mol. Cell 62:295-306(2016).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=DGCC8004;
RX   PubMed=28663439; DOI=10.1126/science.aao0100;
RA   Kazlauskiene M., Kostiuk G., Venclovas C., Tamulaitis G., Siksnys V.;
RT   "A cyclic oligonucleotide signaling pathway in type III CRISPR-Cas
RT   systems.";
RL   Science 357:605-609(2017).
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). The
CC       type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC       RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC       cognate to the crRNA is required for all activities. In a heterologous
CC       host this Csm effector complex restricts ssRNA phage MS2, suggesting it
CC       may target RNA viruses in vivo. {ECO:0000269|PubMed:25458845}.
CC   -!- FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between
CC       crRNA and target RNA to form a ternary Csm complex activates a ssDNase
CC       activity; target RNA cleavage suppresses the ssDNase, a temporal
CC       control that prevents uncontrolled DNA degradation. Viral RNA
CC       transcripts probably tether the Csm complex to the viral genome,
CC       recruiting Cas10 ssDNA activity which is able to degrade DNA in the
CC       transcription bubble, spatially controlling the DNase activity.
CC       {ECO:0000269|PubMed:27105119}.
CC   -!- FUNCTION: This subunit might be involved in maturation of a crRNA
CC       intermediate to its mature form. {ECO:0000305|PubMed:25458845}.
CC   -!- SUBUNIT: Part of the Csm effector complex that includes at least
CC       Cas10(1), Csm2(3), Csm3(5), Csm4(1), Csm5(1) and mature crRNA
CC       (PubMed:25458845, PubMed:27105119, PubMed:28663439). The Csm complex is
CC       elongated and slightly twisted with a maximal length of 215 Angstroms
CC       and a diameter of 75-80 Angstroms (PubMed:25458845). It has been
CC       modeled to have a central protein filamant of Csm3 subunits along which
CC       the dsRNA helix of paired crRNA and target RNA binds. The filament is
CC       capped at one end by Cas10 and Csm4 and at the other end by Csm5; ssDNA
CC       is thought to bind to the N-terminal HD domain of Cas10 (Probable). Csm
CC       with a precursor crRNA does not include Csm5, while Cas6, the enzyme
CC       probably involved in pre-crRNA processing, is found associated with a
CC       subset of the Csm complex (PubMed:25458845).
CC       {ECO:0000269|PubMed:25458845, ECO:0000269|PubMed:27105119,
CC       ECO:0000269|PubMed:28663439, ECO:0000305|PubMed:25458845,
CC       ECO:0000305|PubMed:27105119}.
CC   -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus.
CC       {ECO:0000269|PubMed:25458845}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated Csm5 family.
CC       {ECO:0000305}.
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DR   EMBL; KM222358; AIZ03608.1; -; Genomic_DNA.
DR   RefSeq; WP_014621550.1; NZ_CP049053.1.
DR   AlphaFoldDB; A0A0A7HF79; -.
DR   SMR; A0A0A7HF79; -.
DR   STRING; 322159.STER_0977; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR010173; CRISPR-assoc_Csm5.
DR   InterPro; IPR005537; RAMP_III_fam.
DR   PANTHER; PTHR38007; PTHR38007; 1.
DR   Pfam; PF03787; RAMPs; 1.
DR   TIGRFAMs; TIGR01899; cas_TM1807_csm5; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; RNA-binding.
FT   CHAIN           1..357
FT                   /note="CRISPR system Cms protein Csm5"
FT                   /id="PRO_0000446124"
SQ   SEQUENCE   357 AA;  41161 MW;  51C66D957D73F157 CRC64;
     MKNDYRTFKL SLLTLAPIHI GNGEKYTSRE FIYENKKFYF PDMGKFYNKM VEKRLAEKFE
     AFLIQTRPNA RNNRLISFLN DNRIAERSFG GYSISETGLE SDRNPNSAGA INEVNKFIRD
     AFGNPYIPGS SLKGAIRTIL MNTTPKWNNE NAVNDFGRFP KENKNLIPWG PKKGKEYDDL
     FNAIRVSDSK PFDNKRLILV QKWDYSAKTN KAKPLPLYRE SISPLTKIEF EITTTTDEAG
     RLIEELGKRA QAFYKDYKAF FLSEFPDDKI QANLQYPIYL GAGSGAWTKT LFKQADGILQ
     RRYSRMKTKM VKKGVLKLTK APLKIVKIPS GNHSLIKNHE SFYEMGKANF MIKEIDK