ID   NTPPB_NEIMB             Reviewed;         196 AA.
AC   Q9JXS2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=7-methyl-GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            Short=m(7)GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00528};
GN   OrderedLocusNames=NMB1909;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-
CC       methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and
CC       in preventing the incorporation of modified nucleotides into cellular
CC       nucleic acids. {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP;
CC         Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- SIMILARITY: Belongs to the Maf family. YceF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
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DR   EMBL; AE002098; AAF42239.1; -; Genomic_DNA.
DR   PIR; D81028; D81028.
DR   RefSeq; NP_274903.1; NC_003112.2.
DR   RefSeq; WP_002221554.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXS2; -.
DR   SMR; Q9JXS2; -.
DR   STRING; 122586.NMB1909; -.
DR   PaxDb; Q9JXS2; -.
DR   EnsemblBacteria; AAF42239; AAF42239; NMB1909.
DR   KEGG; nme:NMB1909; -.
DR   PATRIC; fig|122586.8.peg.2435; -.
DR   HOGENOM; CLU_040416_1_0_4; -.
DR   OMA; CAGSFKA; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..196
FT                   /note="7-methyl-GTP pyrophosphatase"
FT                   /id="PRO_0000123034"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            15
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            73
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            158
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   196 AA;  21911 MW;  C545A16B978561E9 CRC64;
     MGLELPLILG TSSVFRREQM ERLGIAFQAA SPDFDETPML GESAPQTALR LAEGKARSLT
     GRFPEALIVG ADQVAWCDGR QWGKPMNLAN AQKMLMHLSG REIEFYSAIV LLNTVTGRMR
     RHIDKTVVVM RQLDELHILR YLEREPDAVY CSCALKSEDL GALLIERIES TDPNALIGLP
     VFRLVDFLKN EGVEVL