NUCC_VIBMT
ID NUCC_VIBMT Reviewed; 245 AA.
AC P0DUD6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=CRISPR-associated endodeoxyribonuclease NucC {ECO:0000303|PubMed:31932164};
DE EC=3.1.-.- {ECO:0000269|PubMed:31932164};
GN Name=nucC {ECO:0000303|PubMed:31932164}; OrderedLocusNames=VCJ_003156;
OS Vibrio metoecus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC341;
RA Sims D.R., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6UXF, ECO:0007744|PDB:6UXG}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-241, FUNCTION, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=RC341;
RX PubMed=31932164; DOI=10.1016/j.molcel.2019.12.010;
RA Lau R.K., Ye Q., Birkholz E.A., Berg K.R., Patel L., Mathews I.T.,
RA Watrous J.D., Ego K., Whiteley A.T., Lowey B., Mekalanos J.J.,
RA Kranzusch P.J., Jain M., Pogliano J., Corbett K.D.;
RT "Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial
RT Endonuclease Mediating Bacteriophage Immunity.";
RL Mol. Cell 77:723-733(2020).
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|PubMed:31932164}.
CC -!- FUNCTION: A cyclic nucleotide-activated dsDNase. In the presence of
CC 3',3',3'-cyclic AMP-AMP-AMP (cAAA), and to a much lesser extent
CC 3',3',3'-cyclic AMP-AMP-GMP (cAAG) and cyclic-di-AMP (c-di-AMP),
CC endonucleolytically degrades dsDNA. The nuclease digests dsDNA to about
CC 50 bp lengths. Not stimulated by cGAMP or linear di-AMP
CC (PubMed:31932164). DNA has been modeled to contact a pair of juxtaposed
CC active sites (one from each layer of the hexamer), accounting for
CC cleavage on both strands (By similarity).
CC {ECO:0000250|UniProtKB:D7Y2H5, ECO:0000269|PubMed:31932164}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:D7Y2H5};
CC -!- ACTIVITY REGULATION: Activated by cAAA and to a lesser extent cAA; cAAA
CC binding promotes hexamerization which is probably necessary for
CC nuclease activation. {ECO:0000269|PubMed:31932164}.
CC -!- SUBUNIT: Forms homotrimers and homohexamers; in the presence of cAAA
CC only the homohexamers of face-to-face associated trimers are formed
CC (PubMed:31932164). The 2 cAAA-binding sites are on the exterior of the
CC hexamer at the three-way junction, there are maximally 2 cyclic
CC nucleotides per hexamer (Probable). {ECO:0000269|PubMed:31932164,
CC ECO:0000305|PubMed:31932164}.
CC -!- MISCELLANEOUS: Encoded in a type III-B CRISPR locus.
CC {ECO:0000303|PubMed:31932164}.
CC -!- SIMILARITY: Belongs to the NucC endonuclease family.
CC {ECO:0000305|PubMed:31932164}.
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DR EMBL; ACZT01000026; EEX64622.1; -; Genomic_DNA.
DR RefSeq; WP_000046098.1; NZ_NMST01000011.1.
DR PDB; 6UXF; X-ray; 1.65 A; A=2-241.
DR PDB; 6UXG; X-ray; 2.15 A; A/B/C=2-244.
DR PDBsum; 6UXF; -.
DR PDBsum; 6UXG; -.
DR AlphaFoldDB; P0DUD6; -.
DR SMR; P0DUD6; -.
DR GeneID; 66941656; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding.
FT CHAIN 1..245
FT /note="CRISPR-associated endodeoxyribonuclease NucC"
FT /id="PRO_0000451847"
FT ACT_SITE 74
FT /evidence="ECO:0000305|PubMed:31932164"
FT ACT_SITE 105
FT /evidence="ECO:0000305|PubMed:31932164"
FT ACT_SITE 107
FT /evidence="ECO:0000305|PubMed:31932164"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:31932164"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:31932164"
FT SITE 54
FT /note="Binds cAAA"
FT /evidence="ECO:0000305|PubMed:31932164"
FT SITE 82
FT /note="Binds cAAA"
FT /evidence="ECO:0000305|PubMed:31932164"
FT SITE 137
FT /note="Gate loop latch"
FT /evidence="ECO:0000305|PubMed:31932164"
FT SITE 142
FT /note="Gate loop latch"
FT /evidence="ECO:0000305|PubMed:31932164"
FT SITE 226
FT /note="Binds cAAA"
FT /evidence="ECO:0000305|PubMed:31932164"
FT HELIX 7..30
FT /evidence="ECO:0007829|PDB:6UXF"
FT TURN 32..38
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6UXF"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6UXF"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:6UXF"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:6UXF"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6UXF"
SQ SEQUENCE 245 AA; 28033 MW; A5795C4E49F6F800 CRC64;
MAQDWQLSEL LENLHADVQH KLTTVRKSFK HSVVKGDGAE NVWVDLFNQY LPERYRASRA
FVVDSENQFS EQIDVVIYDR QYSPFIFHYA EQLIIPAESV YAVFEVKQTL NKQHIDAARK
KVASVRALHR TSLPIPHAGG VHSPRELIGI IGGLLTLENE LKIPDTLMGH LDHDKADKGM
LNIGCAADDC FFYYDNDHQR MQVMQHKKAT TAFLFELLSQ LQKCGTVPMI DIHAYGKWLT
PRISE
