MAZG_ECO57
ID MAZG_ECO57 Reviewed; 263 AA.
AC P0AEY4; P33646;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase;
DE Short=NTP-PPase;
DE EC=3.6.1.8;
GN Name=mazG; OrderedLocusNames=Z4096, ECs3641;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in the regulation of bacterial cell survival under
CC conditions of nutritional stress. Regulates the MazE-MazF toxin-
CC antitoxin (TA) system that mediates programmed cell death (PCD). This
CC is achieved by lowering the cellular concentration of (p)ppGpp produced
CC by RelA under amino acid starvation, thus protecting the cell from the
CC toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct
CC degradation of (p)ppGpp or by degradation of NTPs, which are substrates
CC for (p)ppGpp synthesis by RelA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57894.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37064.1; -; Genomic_DNA.
DR PIR; A98084; A98084.
DR PIR; B85929; B85929.
DR RefSeq; NP_311668.1; NC_002695.1.
DR RefSeq; WP_001071648.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEY4; -.
DR SMR; P0AEY4; -.
DR STRING; 155864.EDL933_3959; -.
DR DNASU; 958247; -.
DR EnsemblBacteria; AAG57894; AAG57894; Z4096.
DR EnsemblBacteria; BAB37064; BAB37064; ECs_3641.
DR GeneID; 66673352; -.
DR GeneID; 916566; -.
DR KEGG; ece:Z4096; -.
DR KEGG; ecs:ECs_3641; -.
DR PATRIC; fig|386585.9.peg.3805; -.
DR eggNOG; COG3956; Bacteria.
DR HOGENOM; CLU_038356_0_1_6; -.
DR OMA; HPHIYGD; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047693; F:ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR004518; MazG_cat.
DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
DR PANTHER; PTHR30522; PTHR30522; 1.
DR Pfam; PF03819; MazG; 2.
DR TIGRFAMs; TIGR00444; mazG; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..263
FT /note="Nucleoside triphosphate pyrophosphohydrolase"
FT /id="PRO_0000096249"
FT BINDING 168..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 30412 MW; C396BC3B9378D2BE CRC64;
MNQIDRLLTI MQRLRDPENG CPWDKEQTFA TIAPYTLEET YEVLDAIARE DFDDLRGELG
DLLFQVVFYA QMAQEEGRFD FNDICAAISD KLERRHPHVF ADSSAENSSE VLARWEQIKT
EERAQKAQHS ALDDIPRSLP ALMRAQKIQK RCANVGFDWT TLGPVVDKVY EEIDEVMYEA
RQAVVDQAKL EEEMGDLLFA TVNLARHLGT KAEIALQKAN EKFERRFREV ERIVAARGLE
MTGVDLETME EVWQQVKRQE IDL
