CSM6_ENTI1
ID CSM6_ENTI1 Reviewed; 430 AA.
AC E6LHV2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=CRISPR system endoribonuclease Csm6;
DE EC=3.1.-.- {ECO:0000269|PubMed:28722012};
DE AltName: Full=CRISPR type III-A associated protein Csm6 {ECO:0000305};
GN Name=csm6; ORFNames=HMPREF9088_1942;
OS Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=888064;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5;
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN PHAGE RESISTANCE, FUNCTION AS AN ENDORIBONUCLEASE, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF GLN-116 AND 372-ARG-ASN-373.
RC STRAIN=DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5;
RX PubMed=28722012; DOI=10.1038/nature23467;
RA Niewoehner O., Garcia-Doval C., Rostoel J.T., Berk C., Schwede F.,
RA Bigler L., Hall J., Marraffini L.A., Jinek M.;
RT "Type III CRISPR-Cas systems produce cyclic oligoadenylate second
RT messengers.";
RL Nature 548:543-548(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)
CC (Probable). The type III-A Csm effector complex binds crRNA and acts as
CC a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding
CC of target RNA cognate to the crRNA is required for all activities. In a
CC heterologous host the appropriately targeted Csm effector complex
CC prevents growth of dsDNA phage phiNM1-gamma6. This protein is not part
CC of the Csm effector complex (PubMed:28722012).
CC {ECO:0000269|PubMed:28722012, ECO:0000305}.
CC -!- FUNCTION: A single-strand-specific endoribonuclease (ssRNase)
CC (PubMed:28722012). Activity is stimulated by cyclic oligoadenylates
CC (cOA); maximal stimulation is seen with cyclic hexaadenylate (cA6)
CC (PubMed:28722012). {ECO:0000269|PubMed:28722012}.
CC -!- ACTIVITY REGULATION: Non-specific ssRNase activity is allosterically
CC activated by cyclic hexaadenylate (cA6) binding to its CARF domain. cA6
CC is a second messenger produced by Cas10 of the ternary Csm effector
CC complex in the presence of a cognate target RNA.
CC {ECO:0000269|PubMed:28722012}.
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 cA6 effector. ssRNase activity resides in the C-terminal HEPN
CC domain. {ECO:0000250|UniProtKB:Q53W17}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus.
CC {ECO:0000305|PubMed:28722012}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm6 family.
CC {ECO:0000305}.
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DR EMBL; AEPV01000074; EFU73212.1; -; Genomic_DNA.
DR RefSeq; WP_007208953.1; NZ_JXKT01000007.1.
DR PDB; 6TUG; X-ray; 2.42 A; A/B/C/D/E/F/G/H=1-430.
DR PDBsum; 6TUG; -.
DR AlphaFoldDB; E6LHV2; -.
DR SMR; E6LHV2; -.
DR STRING; 888064.HMPREF9088_1942; -.
DR EnsemblBacteria; EFU73212; EFU73212; HMPREF9088_1942.
DR PATRIC; fig|888064.11.peg.2080; -.
DR eggNOG; ENOG502Z9RR; Bacteria.
DR HOGENOM; CLU_047385_3_0_9; -.
DR OMA; NIGHDND; -.
DR OrthoDB; 378705at2; -.
DR Proteomes; UP000010296; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome.
FT CHAIN 1..430
FT /note="CRISPR system endoribonuclease Csm6"
FT /id="PRO_0000446125"
FT REGION 1..155
FT /note="CARF domain"
FT /evidence="ECO:0000305|PubMed:28722012"
FT REGION 156..430
FT /note="HEPN domain"
FT /evidence="ECO:0000305|PubMed:28722012"
FT MUTAGEN 116
FT /note="Q->A: Loss of ssRNase activity in the presence or
FT absence of activator. Does not protect against phage
FT infection in a heterologous host."
FT /evidence="ECO:0000269|PubMed:28722012"
FT MUTAGEN 372..373
FT /note="RN->AA: Loss of ssRNase activity in the presence or
FT absence of activator. Does not protect against phage
FT infection in a heterologous host."
FT /evidence="ECO:0000269|PubMed:28722012"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6TUG"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:6TUG"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 389..407
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:6TUG"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:6TUG"
SQ SEQUENCE 430 AA; 50627 MW; AD4DEDF2578F7141 CRC64;
MKILFSPIGN TDPWRNDRDG AMLHIVRHYQ PDRVVLFFTE SIWQGNQHFS GQQAFDWVKI
IQSINENCQI EIKCDTIEVE NDFDAYKDLF HQYLVEEKRK YPNAEIFLNV TSGTPQMETT
LCLEYVTYPD KMRCIQVSTP LKTSNAKTKY AQADCQEVDL EIVNEEESQQ PSRCHKIAIL
SFREAIVRNQ IKSLLDNYDY EAALQLVASQ KSFRNGKEIR KKLKELIDDI KMHRVFSYLI
KQYPRNEKLQ KALLHTILLE MRHQRGDIAE TLIRVKSIAE YIVEQYIQKN YPYLIIYKED
KPYFNVSYSQ ELTESYLALM DSRNKKTNKK MTVDSLDRIL GFPAYRDFLQ LLEASNEMTN
EMNKVNEINN LRNKVAHNLD SLNLDRDKNG RKITNAVTAV RTMLLAVFPE VQENDFHYLK
QFNQSIKELL
