ID   CAP13_FLASX             Reviewed;         235 AA.
AC   P0DUD7;
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 13 {ECO:0000305};
DE            Short=Cap13 {ECO:0000305};
DE   AltName: Full=TM-STING {ECO:0000303|PubMed:32877915};
DE            Short=FsSTING {ECO:0000303|PubMed:32877915};
GN   Name=cap13 {ECO:0000305}; ORFNames=Ga0077528_101611, IMG 2624319773;
OS   Flavobacteriaceae sp. genome_bin_11.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=2778089;
RN   [1]
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   [2] {ECO:0007744|PDB:6WT4}
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 75-235 IN COMPLEX WITH
RP   3'3'-CGAMP, C-DI-GMP-BINDING, NUCLEOTIDE-BINDING, SUBUNIT, AND DOMAIN.
RX   PubMed=32877915; DOI=10.1038/s41586-020-2719-5;
RA   Morehouse B.R., Govande A.A., Millman A., Keszei A.F.A., Lowey B., Ofir G.,
RA   Shao S., Sorek R., Kranzusch P.J.;
RT   "STING cyclic dinucleotide sensing originated in bacteria.";
RL   Nature 586:429-433(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 I-D(GG) CBASS system (PubMed:32839535).
CC       {ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32877915}.
CC   -!- FUNCTION: Binds cyclic dinucleotides: binds c-di-GMP (synthesized by
CC       the cognate CdnE encoded upstream in the same operon), cyclic 3'3'-
CC       cyclic GMP-AMP (3'3'-cGAMP) but not cUMP-AMP (PubMed:32877915). The
CC       effector protein for this CBASS system, its activity is stimulated by
CC       c-di-GMP and leads to cell death (Probable).
CC       {ECO:0000269|PubMed:32877915, ECO:0000305|PubMed:32877915}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32877915}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DOMAIN: The cyclic nucleotide binds in the C-terminal bacterial STING
CC       region (PubMed:32877915). Comparison of structures from 2 different
CC       bacteria suggests that cyclic nucleotide binding causes domain
CC       rotation, which forms a lid and seals the nucleotide-binding pocket
CC       (Probable). {ECO:0000269|PubMed:32877915, ECO:0000305|PubMed:32877915}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the bacterial STING
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=IMG gene page for 2624319773;
CC       URL="https://img.jgi.doe.gov/cgi-bin/m/main.cgi?section=GeneDetail&page=genePageMainFaa&gene_oid=2624319773";
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   PDB; 6WT4; X-ray; 1.78 A; A/B=75-235.
DR   PDBsum; 6WT4; -.
DR   AlphaFoldDB; P0DUD7; -.
DR   SMR; P0DUD7; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..235
FT                   /note="CD-NTase-associated protein 13"
FT                   /id="PRO_0000451882"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           80..91
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           93..102
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           123..135
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          155..161
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           172..176
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           177..181
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   HELIX           194..218
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:6WT4"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:6WT4"
SQ   SEQUENCE   235 AA;  27142 MW;  7624B5179A6C1599 CRC64;
     MEKIYTWLKT NSYIVHHVST SLNIISFIIV LIWIFESTIK EKLNIIFTVN LEAIVVFISI
     LIVGLNQLLQ KLLIEAEYSP AFALAVGYFK NFIFPAITQI KENGEVNPKI CIYKPKHFDE
     LTSTNIDMIK AELTNKKYNL SEINLSLKGA RARDILTLNK KSKIHSYFDF PNTLLSLYSY
     VDFKIASSNN NSSELKKKKF VELLIEQFYL KLNELIQENN LTNNITFCDK NLQGL