ID   CAP6_PSEAI              Reviewed;         304 AA.
AC   P0DTF4;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=CD-NTase-associated protein 6 {ECO:0000303|PubMed:32839535};
DE            Short=Cap6 {ECO:0000303|PubMed:32839535};
DE   AltName: Full=CBASS disassembly protein Trip13 {ECO:0000303|PubMed:31932165};
DE   AltName: Full=Probable ATPase Trip13 {ECO:0000303|PubMed:31932165};
GN   Name=cap6 {ECO:0000303|PubMed:32839535};
GN   Synonyms=trip13 {ECO:0000303|PubMed:31932165}; ORFNames=A4W92_29520;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27853 / DSM 1117 / CIP 76.110 / JCM 6119 / LMG 6395 / NCIMB
RC   12469;
RX   PubMed=27139485; DOI=10.1128/aac.00434-16;
RA   Feng Y., Jonker M.J., Moustakas I., Brul S., Ter Kuile B.H.;
RT   "Dynamics of Mutations during Development of Resistance by Pseudomonas
RT   aeruginosa against Five Antibiotics.";
RL   Antimicrob. Agents Chemother. 60:4229-4236(2016).
RN   [2]
RP   FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-78 AND GLU-143.
RC   STRAIN=ATCC 27853 / DSM 1117 / CIP 76.110 / JCM 6119 / LMG 6395 / NCIMB
RC   12469;
RX   PubMed=31932165; DOI=10.1016/j.molcel.2019.12.009;
RA   Ye Q., Lau R.K., Mathews I.T., Birkholz E.A., Watrous J.D., Azimi C.S.,
RA   Pogliano J., Jain M., Corbett K.D.;
RT   "HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-
RT   like Enzymes to Mediate Bacteriophage Immunity.";
RL   Mol. Cell 77:709-722(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 III-C(AAA) CBASS system (PubMed:32839535).
CC       {ECO:0000269|PubMed:31932165, ECO:0000303|PubMed:32839535}.
CC   -!- FUNCTION: Prevents the CdnD:Cap7:Cap8 complex (also called
CC       CdnD:HORMA2:HORMA3) from synthesizing 2',3',3'-cyclic AMP-AMP-AMP
CC       (cAAA) (PubMed:31932165). Binds and disassembles an active
CC       CdnD:Cap7:Cap8 complex, inhibiting the complex's ability to synthesize
CC       cyclic nucleotide second messengers. An AAA+-ATPase remodeler, it is
CC       thought that in the absence of foreign threat Cap6 maintains the Cap7
CC       protein in an open, inactive state. Once activated (presumably by a
CC       bacteriophage protein) Cap7 binds to and activates its cognate CD-NTase
CC       (CdnD in this bacteria) to synthesize cAAA, a cyclic nucleotide second
CC       messenger. cAAA activates the NucC endonuclease which degrades all DNA
CC       in the infected cell, causing cell death and abortive phage infection
CC       (Probable). {ECO:0000269|PubMed:31932165, ECO:0000305|PubMed:31932165}.
CC   -!- SUBUNIT: Oligomerizes (PubMed:31932165). Homohexamer. Forms a 1:1:6
CC       CdnD:Cap7:Cap6 complex (Probable). {ECO:0000269|PubMed:31932165,
CC       ECO:0000305|PubMed:31932165}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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; CP015117; AMX91003.1; -; Genomic_DNA.
DR   RefSeq; WP_016852809.1; NZ_WXZT01000006.1.
DR   AlphaFoldDB; P0DTF4; -.
DR   SMR; P0DTF4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044539; Pch2-like.
DR   PANTHER; PTHR45991; PTHR45991; 1.
DR   Pfam; PF00004; AAA; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Nucleotide-binding.
FT   CHAIN           1..304
FT                   /note="CD-NTase-associated protein 6"
FT                   /id="PRO_0000451844"
FT   BINDING         75..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:D7Y2H4"
FT   MUTAGEN         78
FT                   /note="K->A: No longer prevents second messenger
FT                   synthesis."
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   MUTAGEN         143
FT                   /note="E->Q: No longer prevents second messenger
FT                   synthesis."
FT                   /evidence="ECO:0000269|PubMed:31932165"
SQ   SEQUENCE   304 AA;  32629 MW;  A0488E9623FE434E CRC64;
     MTKNPSSDAT LPKGIHRSWK LPDKSLGDLW DSIVMDEAIK KQLLSQAIVN FTVRPKVERT
     VLPLHGVILL VGPPGTGKTS LARGLAHRVA ESFSSAKFRL LEVEPHTLTS SAMGKTQRAV
     ADLFSQSIAE SAAAGPTIVL LDEVETLAAD RAKLSLEANP VDVHRATDAV LVQLDMLAER
     NPHLLFVATS NFPQAVDSAF LSRCDMVMEV PLPGKDACKQ ILVDCLNGLA KTFPGIGKLS
     SAHQFDVCAG ECVGLDGRAI RKVVANALAA DPQVAIDPNK LSVEHLRSAI RQAKQMRLQG
     GKQK