HEPT_THECF
ID HEPT_THECF Reviewed; 110 AA.
AC I3ZRF2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Probable ribonuclease HepT;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE AltName: Full=Toxin HepT {ECO:0000303|PubMed:33045733};
GN Name=hepT {ECO:0000303|PubMed:33045733}; ORFNames=CL1_0071;
OS Thermococcus cleftensis (strain DSM 27260 / KACC 17922 / CL1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=163003;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27260 / KACC 17922 / CL1;
RX PubMed=22887670; DOI=10.1128/jb.01016-12;
RA Jung J.H., Holden J.F., Seo D.H., Park K.H., Shin H., Ryu S., Lee J.H.,
RA Park C.S.;
RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT sp. Strain CL1, Isolated from a Paralvinella sp. Polychaete Worm Collected
RT from a Hydrothermal Vent.";
RL J. Bacteriol. 194:4769-4770(2012).
RN [2]
RP FUNCTION AS A TOXIN, PROBABLE AMPYLATION AT TYR-82, AND MUTAGENESIS OF
RP TYR-82.
RC STRAIN=DSM 27260 / KACC 17922 / CL1;
RX PubMed=33045733; DOI=10.1093/nar/gkaa855;
RA Yao J., Zhen X., Tang K., Liu T., Xu X., Chen Z., Guo Y., Liu X.,
RA Wood T.K., Ouyang S., Wang X.;
RT "Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT
RT toxin/antitoxin system.";
RL Nucleic Acids Res. 48:11054-11067(2020).
CC -!- FUNCTION: Toxic component of a type VII toxin-antitoxin (TA) system.
CC Overexpression in E.coli inhibits cell growth. Neutralized by cognate
CC antitoxin MntA (PubMed:33045733). Neutralization is probably due to
CC AMPylation by MntA (Probable). Probably an RNAase (By similarity).
CC {ECO:0000250|UniProtKB:Q8ECH6, ECO:0000269|PubMed:33045733,
CC ECO:0000305|PubMed:33045733}.
CC -!- PTM: Modified by cognate antitoxin MntA; probably at least 2 successive
CC AMPylation events occur on Tyr-82. {ECO:0000269|PubMed:33045733}.
CC -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
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DR EMBL; CP003651; AFL94286.1; -; Genomic_DNA.
DR RefSeq; WP_014787927.1; NC_018015.1.
DR AlphaFoldDB; I3ZRF2; -.
DR SMR; I3ZRF2; -.
DR STRING; 163003.CL1_0071; -.
DR EnsemblBacteria; AFL94286; AFL94286; CL1_0071.
DR GeneID; 13038727; -.
DR KEGG; thm:CL1_0071; -.
DR HOGENOM; CLU_142825_3_3_2; -.
DR OrthoDB; 112390at2157; -.
DR Proteomes; UP000006064; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR InterPro; IPR008201; HepT-like.
DR Pfam; PF01934; DUF86; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nuclease; Nucleotide-binding; Phosphoprotein;
KW Toxin-antitoxin system.
FT CHAIN 1..110
FT /note="Probable ribonuclease HepT"
FT /id="PRO_0000452434"
FT MOTIF 75..82
FT /note="RX(4)HXY motif"
FT /evidence="ECO:0000269|PubMed:33045733"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT ACT_SITE 80
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT MOD_RES 82
FT /note="O-di-AMP-tyrosine"
FT /evidence="ECO:0000305|PubMed:33045733"
FT MUTAGEN 82
FT /note="Y->F: Remains toxic, no longer modified by MntA."
FT /evidence="ECO:0000269|PubMed:33045733"
SQ SEQUENCE 110 AA; 13166 MW; A870573A7B215932 CRC64;
MKRSHKDYLE DIAEAIELIE EFTREICFED FLCDKKTQFA VIRALEIIGE ASKNIPNDFK
RLHPEIPWRE MARMRDKLIH AYFGVDVRVL WKTVKEDIPS LKGKFEKLRK
