CAP8_PSEAI
ID CAP8_PSEAI Reviewed; 156 AA.
AC P0DTF5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=CD-NTase-associated protein 8 {ECO:0000303|PubMed:32839535};
DE Short=Cap8 {ECO:0000303|PubMed:32839535};
DE AltName: Full=Bacterial HORMA3 protein {ECO:0000303|PubMed:31932165};
GN Name=cap8 {ECO:0000303|PubMed:32839535};
GN Synonyms=HORMA3 {ECO:0000303|PubMed:31932165}; ORFNames=A4W92_29525;
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 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 [3] {ECO:0007744|PDB:6P8P, ECO:0007744|PDB:6P8S}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 2-133 ALONE AND IN COMPLEX WITH
RP CAP7, FUNCTION, SUBUNIT, AND DOMAIN.
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).
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: A member of the CBASS system in this bacteria. It does not
CC seem to bind a closure peptide, its exact function is unknown.
CC {ECO:0000269|PubMed:31932165}.
CC -!- SUBUNIT: Interacts with Cap7 (also called HORMA2) and CdnC; forms
CC CdnD:Cap7:Cap8 (also called CdnD:HORMA2:HORMA3) complexes with
CC stoichiometries of 1:1:1 and 2:1:1. {ECO:0000269|PubMed:31932165}.
CC -!- DOMAIN: Does not seem to be able to assume a closed conformation, does
CC not bind closure peptide. In the Cap7:Cap8 complex only Cap7 binds a
CC closure peptide. {ECO:0000269|PubMed:31932165}.
CC -!- SIMILARITY: Belongs to the bacterial HORMA family. HORMA3 subfamily.
CC {ECO:0000305|PubMed:31932165}.
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DR EMBL; CP015117; AMX91004.1; -; Genomic_DNA.
DR RefSeq; WP_003090160.1; NZ_WXZT01000006.1.
DR PDB; 6P8P; X-ray; 1.64 A; A/B/C/D=2-134.
DR PDB; 6P8S; X-ray; 2.00 A; C/D=2-133.
DR PDBsum; 6P8P; -.
DR PDBsum; 6P8S; -.
DR AlphaFoldDB; P0DTF5; -.
DR SMR; P0DTF5; -.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense.
FT CHAIN 1..156
FT /note="CD-NTase-associated protein 8"
FT /id="PRO_0000451842"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6P8P"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6P8P"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6P8P"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6P8P"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6P8P"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6P8P"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6P8S"
SQ SEQUENCE 156 AA; 16652 MW; E82968D735061866 CRC64;
MTTVVSRTFR SSPHRDALQT WDAIVELLTQ GKDGTARSEL RAVTGVAASL IADQAPKSAP
IVATCDGPRT RIYCLFDEDA IDGDDANEEV LGFEPLKGDW GVSLPCPKEQ LGWVQSALKK
HSSRIIARDL SQGIATQAQA DAGQALSLDL GGFLKS
