CAP4_ENTCL
ID CAP4_ENTCL Reviewed; 499 AA.
AC P0DUD5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 4.
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=P853_02261 {ECO:0000312|EMBL:EUL38998.1};
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCI 50;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Earl A., Hung D.,
RA Onderdonk A.B., Ferraro M.J., Hooper D., Dekker J., O'Brien T., Huang S.,
RA Quan V., Ernst C., Delaney M., DuBois A., Kim D.S., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterobacter cloacae UCI 50.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS A RECEPTOR, FUNCTION AS AN ENDONUCLEASE, ANTIVIRAL DEFENSE,
RP COFACTOR, ACTIVITY REGULATION, SUBUNIT, DNA-BINDING, NUCLEOTIDE-BINDING,
RP OPERON STRUCTURE, DOMAIN, AND MUTAGENESIS OF 1-MET--HIS-10; LYS-74;
RP ASN-326; HIS-328; PHE-483 AND TYR-493.
RC STRAIN=UCI 50;
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).
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).
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. A type II-C(AAG) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:32544385, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Binds second messenger 3',3',3'-cyclic AMP-AMP-GMP (cAAG). In
CC the presence of 3',3',3'-cyclic AMP-AMP-GMP (synthesized by the cognate
CC CD-NTase protein in the CBASS operon), endonucleolytically degrades
CC dsDNA to approximately 17 bp length fragments, with a preference for
CC 5'-C|NG sites. Only binds DNA in the presence of cAAG. Not activated by
CC c-di-AMP, c-di-GMP, 3'3'-cyclic GMP-AMP (3'3'-cGAMP) or the second
CC messenger of A.baumanii strain ATCC 27244.
CC {ECO:0000269|PubMed:32544385}.
CC -!- FUNCTION: Protects E.coli against phage T2 infection. When the cdnD-
CC cap2-cap3-cap4 operon is introduced in E.coli there is a more than
CC 10(3) decrease in the efficiency of T2 plaque formation. The operon
CC does not protect against phage T5 and only about 10-fold against T7.
CC {ECO:0000269|PubMed:32544385}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:32544385};
CC -!- ACTIVITY REGULATION: DNase activity is activated upon ligand binding.
CC Inhibited by EDTA. {ECO:0000269|PubMed:32544385}.
CC -!- SUBUNIT: A monomer in the absence of ligand, in its presence it forms
CC oligomers. {ECO:0000269|PubMed:32544385}.
CC -!- INDUCTION: Part of the CBASS operon consisting of cap4-cdnD-cap2-cap3.
CC {ECO:0000305|PubMed:32544385}.
CC -!- DOMAIN: The cyclic nucleotide ligand binds in the C-terminal SAVED
CC domain. DNA binding requires the extreme N-terminus.
CC {ECO:0000269|PubMed:32544385}.
CC -!- SIMILARITY: Belongs to the Cap4 nuclease family.
CC {ECO:0000305|PubMed:32544385}.
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DR EMBL; JCKK01000002; EUL38998.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DUD5; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 Antiviral defense; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding.
FT CHAIN 1..499
FT /note="CD-NTase-associated protein 4"
FT /id="PRO_0000451851"
FT REGION 1..226
FT /note="N-terminal endonuclease domain"
FT /evidence="ECO:0000305|PubMed:32544385"
FT REGION 258..464
FT /note="C-terminal SAVED domain"
FT /evidence="ECO:0000305|PubMed:32544385"
FT MUTAGEN 1..10
FT /note="Missing: Required for nuclease activity, still binds
FT cAAG."
FT /evidence="ECO:0000269|PubMed:32544385"
FT MUTAGEN 74
FT /note="K->A: Loss of nuclease activity, still binds cAAG.
FT No longer protects against phage T2."
FT /evidence="ECO:0000269|PubMed:32544385"
FT MUTAGEN 326
FT /note="N->A: Slight reduction in DNase activity."
FT /evidence="ECO:0000269|PubMed:32544385"
FT MUTAGEN 328
FT /note="H->A: No change in DNase activity."
FT /evidence="ECO:0000269|PubMed:32544385"
FT MUTAGEN 483
FT /note="F->A: Reduced DNase activity."
FT /evidence="ECO:0000269|PubMed:32544385"
FT MUTAGEN 493
FT /note="Y->A: Greatly reduced DNase activity."
FT /evidence="ECO:0000269|PubMed:32544385"
SQ SEQUENCE 499 AA; 56198 MW; 0A6E034D42B89F21 CRC64;
MATSVLANWH GHDYQARYFW IEASRLKNPQ QDFVVEVSYE ADGPKAFDDV ITRYNPPRRS
TGPDRIQADY YQIKFHVTQA ASFGFEDLID PAFIGAETFS ILERLKQAKG TEPANSAFHL
VTTDRIIDED PLGEIISNVD GSIRLDKLFD GTTDRSRKGK VRKLWRQHLK LSTDQELEQV
LSGFHIQQSQ PTLEAMREKV NTCFQIIGLI TCETSSDFRF DGAARALRSQ ERYRFTREQF
TALCEEENWI RSEAPESFRN VALRSFSDGP LDIMDALPEH TLSLLSLFEG RFPSPGIEWN
DVIKPQVETF LTGIRQTERK VRLYLNTHSS IAMLAGKCLG HKSGVEIELV QKGRMGDSIW
SENESQDEPD AVIETETVGT GSDVAVVLSI TRNALPKARA YILENQPDIG RIIHVTPANG
HGQRSVKNGS HAVAIAEQVS DVVMDADLPV EASLHIFSAA PNAVNFYLGQ HTDFLGTCVF
YEFDFQRQRD GSYLPSFKV
