ID   NTPPB_SHIFL             Reviewed;         194 AA.
AC   P0A730; P27244;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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   Name=yceF; OrderedLocusNames=SF1091, S1171;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Maf family. YceF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN42710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP16598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN42710.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP16598.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_707003.3; NC_004337.2.
DR   RefSeq; WP_001125202.1; NZ_WHSI01000003.1.
DR   AlphaFoldDB; P0A730; -.
DR   SMR; P0A730; -.
DR   STRING; 198214.SF1091; -.
DR   PRIDE; P0A730; -.
DR   EnsemblBacteria; AAN42710; AAN42710; SF1091.
DR   EnsemblBacteria; AAP16598; AAP16598; S1171.
DR   GeneID; 1024042; -.
DR   GeneID; 66670647; -.
DR   KEGG; sfl:SF1091; -.
DR   KEGG; sfx:S1171; -.
DR   PATRIC; fig|198214.7.peg.1279; -.
DR   HOGENOM; CLU_040416_1_0_6; -.
DR   OrthoDB; 1469203at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro.
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..194
FT                   /note="7-methyl-GTP pyrophosphatase"
FT                   /id="PRO_0000122980"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            12
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            70
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            154
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   CONFLICT        53
FT                   /note="A -> S (in Ref. 2; AAP16598)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  21691 MW;  DC1BBC4BDD78E9EA CRC64;
     MPKLILASTS PWRRALLEKL QISFECAAPE VDETPRSDES PRQLVLRLAQ EKAQSLASRY
     PDHLIIGSDQ VCVLDGEITG KPLTEENARL QLRKASGNIV TFYTGLALFN SANGHLQTEV
     EPFDVHFRHL SEAEIDNYVR KEHPLHCAGS FKSEGFGITL FERLEGRDPN TLVGLPLIAL
     CQMLRREGKN PLMG