MNTA_THECF
ID MNTA_THECF Reviewed; 99 AA.
AC I3ZRF1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Protein adenylyltransferase MntA;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:33045733};
DE AltName: Full=Antitoxin MntA {ECO:0000303|PubMed:33045733};
GN Name=mntA {ECO:0000303|PubMed:33045733}; ORFNames=CL1_0070;
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 AN ANTITOXIN, AND MUTAGENESIS OF 33-GLY-SER-34 AND
RP 45-ASP--ASP-47.
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: Antitoxin component of a type VII toxin-antitoxin (TA)
CC system. Overexpression in E.coli neutralizes the toxic effect of
CC cognate toxin HepT. Neutralization is mostly due to AMPylation of the
CC toxin by this enzyme. {ECO:0000269|PubMed:33045733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:33045733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-(5'-adenylyl)-L-tyrosyl-[protein] = diphosphate + O-
CC [5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:66528, Rhea:RHEA-COMP:13846, Rhea:RHEA-COMP:17046,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:167160; Evidence={ECO:0000250|UniProtKB:A0A0B0QJN8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8ECH7};
CC Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:Q8ECH7};
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; CP003651; AFL94285.1; -; Genomic_DNA.
DR AlphaFoldDB; I3ZRF1; -.
DR SMR; I3ZRF1; -.
DR STRING; 163003.CL1_0070; -.
DR EnsemblBacteria; AFL94285; AFL94285; CL1_0070.
DR KEGG; thm:CL1_0070; -.
DR HOGENOM; CLU_130257_10_0_2; -.
DR Proteomes; UP000006064; Chromosome.
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 Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Toxin-antitoxin system; Transferase.
FT CHAIN 1..99
FT /note="Protein adenylyltransferase MntA"
FT /id="PRO_0000452437"
FT MOTIF 33..47
FT /note="GSX(10)DXD motif"
FT /evidence="ECO:0000269|PubMed:33045733"
FT ACT_SITE 45
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJN8"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJN8"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT MUTAGEN 33..34
FT /note="GS->AT: No longer AMPylates HepT, does not
FT neutralize HepT."
FT /evidence="ECO:0000269|PubMed:33045733"
FT MUTAGEN 45..47
FT /note="DVD->EVE: No longer AMPylates HepT."
FT /evidence="ECO:0000269|PubMed:33045733"
SQ SEQUENCE 99 AA; 11261 MW; 9B56D4289006A411 CRC64;
MAMLTLEEIE SILTAHKKEL RERFGVREIG VFGSYVRGEA KEDSDVDILV DFEEIPSLLK
FIELEEYLEA LLGLRVDLVM KSSLKSGIAK TVLREVVYV
