CAP7_PSEAI
ID CAP7_PSEAI Reviewed; 166 AA.
AC P0DTF6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=CD-NTase-associated protein 7 {ECO:0000303|PubMed:32839535};
DE Short=Cap7 {ECO:0000303|PubMed:32839535};
DE AltName: Full=Bacterial HORMA2 sensor protein {ECO:0000303|PubMed:31932165};
GN Name=cap7 {ECO:0000303|PubMed:32839535};
GN Synonyms=HORMA2 {ECO:0000303|PubMed:31932165}; ORFNames=A4W92_29530;
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:6P8O, ECO:0007744|PDB:6P8R, ECO:0007744|PDB:6P8S, ECO:0007744|PDB:6P8U}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-131 IN THE OPEN STATE, X-RAY
RP CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 2-166 IN THE CLOSED STATE WITH CLOSURE
RP PEPTIDE, X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH CDND AND
RP CLOSURE PEPTIDE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-95.
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: The sensor protein for this CBASS system. Binds to a closure
CC peptide (consensus Glu-Val-Met-Glu-Phe-Asn-Pro), which allows it to
CC activate CdnD for second messenger synthesis.
CC {ECO:0000305|PubMed:31932165}.
CC -!- SUBUNIT: Interacts individually with CdnD and Cap8 (also called
CC HORMA3); forms CdnD:Cap7:Cap8 (also called CdnD:HORMA2:HORMA3)
CC complexes with stoichiometries of 1:1:1 and 2:1:1.
CC {ECO:0000269|PubMed:31932165}.
CC -!- DOMAIN: Can adopt both open and closed states. Full-length closed state
CC protein binds a closure peptide (consensus Glu-Val-Met-Glu-Phe-Asn-
CC Pro). In the Cap7:Cap8 complex only Cap7 binds a closure peptide.
CC {ECO:0000269|PubMed:31932165}.
CC -!- SIMILARITY: Belongs to the bacterial HORMA family. HORMA2 subfamily.
CC {ECO:0000305|PubMed:31932165}.
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DR EMBL; CP015117; AMX91005.1; -; Genomic_DNA.
DR RefSeq; WP_003090159.1; NZ_WXZT01000006.1.
DR PDB; 6P8O; X-ray; 1.60 A; A/B=2-131.
DR PDB; 6P8R; X-ray; 2.14 A; A/B/C/D=2-166.
DR PDB; 6P8S; X-ray; 2.00 A; A/B=5-166.
DR PDB; 6P8U; X-ray; 1.89 A; B=2-166.
DR PDBsum; 6P8O; -.
DR PDBsum; 6P8R; -.
DR PDBsum; 6P8S; -.
DR PDBsum; 6P8U; -.
DR AlphaFoldDB; P0DTF6; -.
DR SMR; P0DTF6; -.
DR GeneID; 56409848; -.
DR OMA; FRWDIDI; -.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040649; Bact_HORMA.
DR InterPro; IPR036570; HORMA_dom_sf.
DR Pfam; PF18173; bacHORMA_2; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense.
FT CHAIN 1..166
FT /note="CD-NTase-associated protein 7"
FT /id="PRO_0000451841"
FT REGION 134..166
FT /note="Required to bind CdnD"
FT /evidence="ECO:0000269|PubMed:31932165"
FT MUTAGEN 95
FT /note="D->A: Binds to CdnD."
FT /evidence="ECO:0000269|PubMed:31932165"
FT MUTAGEN 95
FT /note="D->K: No longer binds to CdnD."
FT /evidence="ECO:0000269|PubMed:31932165"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6P8O"
FT HELIX 13..31
FT /evidence="ECO:0007829|PDB:6P8O"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:6P8O"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:6P8O"
FT TURN 52..56
FT /evidence="ECO:0007829|PDB:6P8O"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6P8O"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6P8O"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:6P8O"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6P8U"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6P8O"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6P8O"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6P8O"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6P8U"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:6P8U"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:6P8U"
SQ SEQUENCE 166 AA; 18699 MW; 69EF8CE723A00597 CRC64;
MSTVATYSYT HSVTYVTDNI LKSLKDIILL SGLDPEHFAD RWESNTRAIK TWLGTGDLRK
VILEIYNPAT DKLVTRWDID IVYGWSDGDG SFWTDTEQLK YAIKKAGLLP SQAKYKLMLD
TKPGRPDVEG WSKGSYRSTD GMVKQSLGST VEHSGLAGQA GYWRQR
