CAP13_ROSEK
ID CAP13_ROSEK Reviewed; 234 AA.
AC A0A150XSR0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 25-MAY-2022, entry version 13.
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=ReSTING {ECO:0000303|PubMed:32877915};
GN Name=cap13 {ECO:0000305}; ORFNames=MB14_13770;
OS Roseivirga ehrenbergii (strain DSM 102268 / JCM 13514 / KCTC 12282 / NCIMB
OS 14502 / KMM 6017).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=279360;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102268 / JCM 13514 / KCTC 12282 / NCIMB 14502 / KMM 6017;
RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Roseivirga ehrenbergii KMM 6017.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP C-DI-GMP-BINDING, NUCLEOTIDE-BINDING, 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).
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 I-D CBASS(GG) system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32877915}.
CC -!- FUNCTION: Binds c-di-GMP (synthesized by the cognate CdnE encoded
CC upstream in the same operon) and about 10-fold less well 3'3'-cGAMP,
CC but not c-di-AMP, 2'3'-cGAMP or cUMP-AMP (tested with a protein without
CC the transmembrane region) (PubMed:32877915). The effector protein for
CC this CBASS system, its activity is stimulated by c-di-GMP and leads to
CC cell death (Probable). {ECO:0000269|PubMed:32877915,
CC ECO:0000305|PubMed:32877915}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The cyclic nucleotide binds in the C-terminal bacterial STING
CC region. {ECO:0000305|PubMed:32877915}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the bacterial STING
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KYG81645.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LQZQ01000002; KYG81645.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0A150XSR0; -.
DR SMR; A0A150XSR0; -.
DR EnsemblBacteria; KYG81645; KYG81645; MB14_13770.
DR Proteomes; UP000075583; Unassembled WGS sequence.
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 Antiviral defense; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="CD-NTase-associated protein 13"
FT /id="PRO_0000451883"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 27006 MW; 0881E0EA267D7832 CRC64;
MKYGLLQENG KVAEFIQIKT IMKNVIANVS TAITLALMIL WIKYPNRIEW EAIIGILLVI
KEVTIRWQIG KIESLEFSPA ISLAHGYVNN FLEPAINELL MKASNNINFS IYIPHDLEEL
SDQQIDRMKL QIEANGYRLK EIKLKKKTGR PHDLLLVEKQ EGTLSYFDFP RTLLSLQSYI
DYKVDSTKNE FSEEKKIAMG AKLVDAFHNE VDRLIKKKNL EGIVTFVSKD LELY