Y128_METJA
ID Y128_METJA Reviewed; 98 AA.
AC Q57592;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative protein adenylyltransferase MJ0128;
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE AltName: Full=Putative antitoxin MJ0128;
GN OrderedLocusNames=MJ0128;
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 MJ0127 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 MJ0127.
CC {ECO:0000250|UniProtKB:Q8ECH7}.
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; L77117; AAB98108.1; -; Genomic_DNA.
DR PIR; H64315; H64315.
DR RefSeq; WP_010869621.1; NC_000909.1.
DR AlphaFoldDB; Q57592; -.
DR SMR; Q57592; -.
DR STRING; 243232.MJ_0128; -.
DR EnsemblBacteria; AAB98108; AAB98108; MJ_0128.
DR GeneID; 1450970; -.
DR KEGG; mja:MJ_0128; -.
DR eggNOG; arCOG01206; Archaea.
DR HOGENOM; CLU_130257_10_3_2; -.
DR InParanoid; Q57592; -.
DR OMA; YMNLKFY; -.
DR OrthoDB; 108083at2157; -.
DR PhylomeDB; Q57592; -.
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 MJ0128"
FT /id="PRO_0000106706"
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; 11565 MW; 02ED1E679CBDA3AC CRC64;
MKTISEIKDI LRKHKKILKE KYKVKSIAIF GSYARNEQTE KSDIDILVEF YETPDYLKFF
ELEDYLSDLL GIKVDLVIKG AIKNPYIKKS IEEDLIYV
