CSM6_MYCTU
ID CSM6_MYCTU Reviewed; 415 AA.
AC P71635; L0TDF8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 5.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=CRISPR system endoribonuclease Csm6;
DE EC=3.1.-.-;
DE AltName: Full=CRISPR type III-A associated protein Csm6;
GN Name=csm6; OrderedLocusNames=Rv2818c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION IN PLASMID RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=29979631; DOI=10.1096/fj.201800557rr;
RA Wei W., Zhang S., Fleming J., Chen Y., Li Z., Fan S., Liu Y., Wang W.,
RA Wang T., Liu Y., Ren B., Wang M., Jiao J., Chen Y., Zhou Y., Zhou Y.,
RA Gu S., Zhang X., Wan L., Chen T., Zhou L., Chen Y., Zhang X.E., Li C.,
RA Zhang H., Bi L.;
RT "Mycobacterium tuberculosis type III-A CRISPR/Cas system crRNA and its
RT maturation have atypical features.";
RL FASEB J. 33:1496-1509(2019).
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 (Probable). This
CC CRISPR-Cas system protects bacteria against transformation with
CC plasmids containing DNA homologous to its spacer regions
CC (PubMed:29979631). This subunit is a single-strand-specific
CC endoribonuclease (ssRNase) that is stimulated by cyclic oligoadenylates
CC (cOA) produced by the Cas10 subunit of the Csm effector complex (By
CC similarity). {ECO:0000250|UniProtKB:A0A0A7HIX6,
CC ECO:0000269|PubMed:29979631, ECO:0000305|PubMed:29979631}.
CC -!- ACTIVITY REGULATION: Non-specific ssRNase activity is allosterically
CC activated by cyclic oligoadenylates (cOA), a second messenger produced
CC by Cas10 of the ternary Csm effector complex in the presence of a
CC cognate target RNA. {ECO:0000250|UniProtKB:A0A0A7HIX6}.
CC -!- SUBUNIT: Homodimer; the composite ssRNase active site is formed at the
CC dimer interface. {ECO:0000250|UniProtKB:Q53W17}.
CC -!- DOMAIN: The N-terminal CRISPR-associated Rossman fold (CARF) probably
CC binds the cOA effector. ssRNase activity resides in the C-terminal HEPN
CC domain. {ECO:0000250|UniProtKB:Q53W17}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the entire CRISPR-Cas locus (cas6 to
CC cas2, Rv2824c to Rv2816c) decreases resistance to plasmids encoding
CC spacer elements about 6-fold. {ECO:0000269|PubMed:29979631}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm6 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP45618.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45618.1; ALT_INIT; Genomic_DNA.
DR PIR; E70691; E70691.
DR RefSeq; NP_217334.1; NC_000962.3.
DR RefSeq; WP_003899494.1; NC_018143.2.
DR AlphaFoldDB; P71635; -.
DR SMR; P71635; -.
DR STRING; 83332.Rv2818c; -.
DR PaxDb; P71635; -.
DR DNASU; 888510; -.
DR GeneID; 888510; -.
DR KEGG; mtu:Rv2818c; -.
DR PATRIC; fig|83332.12.peg.3143; -.
DR TubercuList; Rv2818c; -.
DR eggNOG; ENOG502Z9RR; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd09699; Csm6_III-A; 1.
DR InterPro; IPR013489; CRISPR-assoc_prot_Csm6.
DR Pfam; PF09659; Cas_Csm6; 1.
DR TIGRFAMs; TIGR02672; cas_csm6; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Endonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..415
FT /note="CRISPR system endoribonuclease Csm6"
FT /id="PRO_0000418229"
FT REGION 1..148
FT /note="CARF domain"
FT /evidence="ECO:0000250|UniProtKB:Q53W17"
FT REGION 149..415
FT /note="HEPN domain"
FT /evidence="ECO:0000250|UniProtKB:Q53W17"
SQ SEQUENCE 415 AA; 46232 MW; 68D92C84485457C1 CRC64;
MILFSPIGTA DPITALGDGP MLHIVRHYRP IVVVLFLSAE IAAFENADRR YSAAITRLAP
ETDVRIVTYT NPSVHRFDLF VPVFRNHLVE LSAEFPDRTI LLNTSSGTPA MQAALVAINV
FGIPRTTAVQ VSTPARALSK PGDRESPDAY DLELMWDAND DNQPGAPNRC FEATSAALGA
LLERANLKQL IVSYDYSAAV TIAADSRLPD QVSNLIRGAM HRSRLEHLVA PKFFKDTAFT
YDPANKVAEY ISALALLAKR EQWAEFARSA TPAITIVLRA AVAKHLPEDR YLDDMGRVDR
RKLEREPEIR CALKHPPKSP NAEWYLYTKD WLALLRQFAP DRVGALEVLG RFESRVRNTA
AHEIVSISED RITKDGGLLP EQLLKILARE TGADLTLYDR LNDEIIRQID MAPLG
