CAP4_MOROS
ID CAP4_MOROS Reviewed; 464 AA.
AC A0A2K8K5C5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=CD-NTase-associated protein 4 {ECO:0000303|PubMed:32544385};
DE Short=Cap4 {ECO:0000303|PubMed:32544385};
DE EC=3.1.-.- {ECO:0000269|PubMed:32544385};
DE AltName: Full=Endodeoxyribonuclease Cap4 {ECO:0000305};
GN Name=cap4 {ECO:0000303|PubMed:32544385};
GN ORFNames=FEF33_11620 {ECO:0000312|EMBL:QCR86478.1},
GN MOTT16_09860 {ECO:0000312|EMBL:ATW86742.1};
OS Moraxella osloensis.
OG Plasmid p2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=34062;
RN [1] {ECO:0000312|Proteomes:UP000232142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TT16 / KCTC 52863; PLASMID=p2;
RX PubMed=29348360; DOI=10.1128/genomea.01509-17;
RA Lim J.Y., Hwang I., Ganzorig M., Huang S.L., Cho G.S., Franz C.M.A.P.,
RA Lee K.;
RT "Complete Genome Sequences of Three Moraxella osloensis Strains Isolated
RT from Human Skin.";
RL Genome Announc. 6:0-0(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOXF1;
RA Brown D.R., Michaels D.L., Kutish G.F., Frasca S. Jr.;
RT "Complete Sequence and Annotation of the Moraxella osloensis Strain MOXF1
RT Genome.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
RN [4] {ECO:0007744|PDB:6VM5}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), FUNCTION AS A NUCLEASE, ACTIVITY
RP REGULATION, SUBUNIT, OPERON STRUCTURE, AND DOMAIN.
RX PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA Kranzusch P.J.;
RT "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL Cell 182:38-49(2020).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection (Probable). A type II-C CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32544385}.
CC -!- FUNCTION: Probably in the presence of its endogenous cyclic nucleotide
CC (synthesized by the cognate CD-NTase protein in the CBASS operon), or
CC of 2',3',3'-cyclic AMP-AMP-AMP (cAAA) synthesized by Acinetobacter sp.
CC ATCC 27244, endonucleolytically degrades dsDNA in a non-sequence
CC specific manner. It is not activated by other cyclic nucleotides.
CC {ECO:0000269|PubMed:32544385}.
CC -!- ACTIVITY REGULATION: DNase activity is activated upon ligand binding.
CC {ECO:0000269|PubMed:32544385}.
CC -!- SUBUNIT: A monomer in the absence of cAAA, in its presence it forms
CC oligomers. {ECO:0000269|PubMed:32544385}.
CC -!- INDUCTION: Part of the CBASS operon consisting of cdnD-cap2-cap3-cap4.
CC {ECO:0000305|PubMed:32544385}.
CC -!- DOMAIN: The cyclic nucleotide ligand binds in the C-terminal SAVED
CC domain. {ECO:0000305|PubMed:32544385}.
CC -!- SIMILARITY: Belongs to the Cap4 nuclease family.
CC {ECO:0000305|PubMed:32544385}.
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DR EMBL; CP024187; ATW86742.1; -; Genomic_DNA.
DR EMBL; CP040257; QCR86478.1; -; Genomic_DNA.
DR RefSeq; WP_060996052.1; NZ_CP024187.1.
DR PDB; 6VM5; X-ray; 2.35 A; A=1-464.
DR PDBsum; 6VM5; -.
DR AlphaFoldDB; A0A2K8K5C5; -.
DR SMR; A0A2K8K5C5; -.
DR EnsemblBacteria; ATW86742; ATW86742; MOTT16_09860.
DR EnsemblBacteria; QCR86478; QCR86478; FEF33_11620.
DR Proteomes; UP000232142; Plasmid p2.
DR GO; GO:0004519; F:endonuclease activity; 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.
DR InterPro; IPR040836; SAVED.
DR Pfam; PF18145; SAVED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding; Plasmid.
FT CHAIN 1..464
FT /note="CD-NTase-associated protein 4"
FT /id="PRO_0000451852"
FT REGION 1..228
FT /note="N-terminal endonuclease domain"
FT /evidence="ECO:0000305|PubMed:32544385"
FT REGION 229..464
FT /note="C-terminal SAVED domain"
FT /evidence="ECO:0000305|PubMed:32544385"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6VM5"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 270..289
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:6VM5"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 396..412
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:6VM5"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:6VM5"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:6VM5"
SQ SEQUENCE 464 AA; 52463 MW; 11D9FB23EFD7BDC5 CRC64;
MSASLLEKQS TGGAIARVGF EYQDAFVLKN LPLWLSESAF SHIVSESIGD VEVCYFSLEK
DFQRVMYEAK NHSLTSTDFW KEIKRFKEAF DIPSSEFTRF GLVCPLYTST LHPFLAQIER
IRGVGSSYSA DSVILQKSRQ DITQWCSDKG FETSLAEFAL DHVDFLSFNA EDSDSVFIGE
IEEKLSNIEL TTRKAKQLRD QFKNLISRSS FGPIHRKDFE NFICHALEED RTQWLSDPIK
INLSASSSQH QDLNLDISDF NGPDRAQKTS SDWNSLIKKA VSIGDFIHNS GDRRTLLIDG
KQRMSTACML GYVFSATRNF LLEIEHNGLA YRTDDHKQKE GQFFNKTNSI ELHGKTEAIV
TIGFPTAIGK DIDSTINEIK NLPRLNLESS NVIDNMETLN LAVKEAKSAL VSFKAENKLS
KLHLFIKAPS VFAMVLGHRL NGVCNIQLYD WVNGEYMPTA ELNI
