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CDND_ACIS2
ID   CDND_ACIS2              Reviewed;         343 AA.
AC   C0VHD2;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Cyclic AMP-AMP-AMP synthase {ECO:0000303|PubMed:32544385};
DE            EC=2.7.7.- {ECO:0000305|PubMed:32544385};
DE   AltName: Full=CD-NTase037 {ECO:0000303|PubMed:30787435};
GN   Name=cdnD01 {ECO:0000303|PubMed:30787435}; ORFNames=HMPREF0023_0551;
OS   Acinetobacter sp. (strain ATCC 27244 / 9458).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=525244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27244 / 9458;
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NOMENCLATURE, AND SIMILARITY.
RC   STRAIN=ATCC 27244 / 9458;
RX   PubMed=30787435; DOI=10.1038/s41586-019-0953-5;
RA   Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R.,
RA   Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y.,
RA   Mekalanos J.J., Kranzusch P.J.;
RT   "Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.";
RL   Nature 567:194-199(2019).
RN   [3]
RP   FUNCTION, AND OPERON STRUCTURE.
RC   STRAIN=ATCC 27244 / 9458;
RX   PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA   Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA   Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA   Kranzusch P.J.;
RT   "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT   cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL   Cell 182:38-49(2020).
RN   [4]
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 II-C(AAAA) CBASS system (PubMed:32839535).
CC       {ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32544385}.
CC   -!- FUNCTION: Cyclic trinucleotide synthase that catalyzes the synthesis of
CC       2',3',3'-cyclic AMP-AMP-AMP as the major product, as well as another
CC       cyclic AMP(4) 2'-5'-linked minor product that acts as a second
CC       messenger for cell signal transduction. {ECO:0000269|PubMed:32544385}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 ATP = 2',3',3'-c-tri-AMP + 3 diphosphate;
CC         Xref=Rhea:RHEA:65488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:156512; Evidence={ECO:0000269|PubMed:32544385};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:G2SLH8};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:G2SLH8};
CC   -!- INDUCTION: Part of the CBASS operon consisting of cdnD-cap2-cap3-cap4.
CC       {ECO:0000305|PubMed:32544385}.
CC   -!- SIMILARITY: Belongs to the CD-NTase family. D01 subfamily.
CC       {ECO:0000305|PubMed:30787435}.
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DR   EMBL; ABYN01000046; EEH69894.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0VHD2; -.
DR   SMR; C0VHD2; -.
DR   STRING; 525244.HMPREF0023_0551; -.
DR   EnsemblBacteria; EEH69894; EEH69894; HMPREF0023_0551.
DR   eggNOG; COG1746; Bacteria.
DR   HOGENOM; CLU_843621_0_0_6; -.
DR   Proteomes; UP000012347; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; ATP-binding; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..343
FT                   /note="Cyclic AMP-AMP-AMP synthase"
FT                   /id="PRO_0000451853"
SQ   SEQUENCE   343 AA;  38347 MW;  F5876DF375FAE76E CRC64;
     MGSERIMTTQ QQFLDLLSDI EPSTTTVNDC SSAHNTLRDA LKVHNEFSKV HVHTFLSGSY
     KRNTAVRPTT IGGITQRPDV DIIALTNHTI NDDPQIVLDA VHTALKDIGY TDLTVNRRSV
     NVKLKKVDMD VVPIISDGYG GYLIPDIHLE EWLVTNPPAH TEWTVEVNKN ANGRFKPLVK
     LFKWWRRENL SDLKRPKGFI LECLVAKHMN YYESNYEKLF VYLLETIRDS YGIYASLGII
     PHLEDPGVAG NNVFSAVTAD EFKTFFEKVE EQAAIARNAL NETDDDKALA LWRQVLGNRF
     PRSASHKSAN SADMASSLIR SALGAGLTFP STPVYPNKPG GFA
 
 
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