Y1217_METJA
ID Y1217_METJA Reviewed; 98 AA.
AC Q58614;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative protein adenylyltransferase MJ1217;
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE AltName: Full=Putative antitoxin MJ1217;
GN OrderedLocusNames=MJ1217;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Probable antitoxin component of a putative type VII toxin-
CC antitoxin (TA) system. Neutralizes cognate toxic MJ1216 by di-
CC AMPylation. {ECO:0000250|UniProtKB:Q8ECH7}.
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:0000250|UniProtKB:Q8ECH7};
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:Q8ECH7};
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 -!- SUBUNIT: Probably forms a complex with cognate toxin MJ1216.
CC {ECO:0000250|UniProtKB:Q8ECH7}.
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; L77117; AAB99218.1; -; Genomic_DNA.
DR PIR; H64451; H64451.
DR RefSeq; WP_010870729.1; NC_000909.1.
DR AlphaFoldDB; Q58614; -.
DR SMR; Q58614; -.
DR STRING; 243232.MJ_1217; -.
DR EnsemblBacteria; AAB99218; AAB99218; MJ_1217.
DR GeneID; 1452113; -.
DR KEGG; mja:MJ_1217; -.
DR eggNOG; arCOG01206; Archaea.
DR HOGENOM; CLU_130257_10_3_2; -.
DR InParanoid; Q58614; -.
DR OMA; YVRQEQT; -.
DR OrthoDB; 108083at2157; -.
DR PhylomeDB; Q58614; -.
DR Proteomes; UP000000805; 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 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Toxin-antitoxin system;
KW Transferase.
FT CHAIN 1..98
FT /note="Putative protein adenylyltransferase MJ1217"
FT /id="PRO_0000107219"
FT MOTIF 31..45
FT /note="GSX(10)DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
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 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
SQ SEQUENCE 98 AA; 11559 MW; 074E10CA476F74D1 CRC64;
MKTLSEIKEI LRKHKKILKE KYKVKSIAIF GSYAREEQKE TSDIDILIDY YEPISLLKLI
ELENYLSDLL GIKVDLITKN SIHNPYVKKS IEEDLIYI
