NTPPB_ECOLI
ID NTPPB_ECOLI Reviewed; 194 AA.
AC P0A729; P27244;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=7-methyl-GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE Short=m(7)GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000269|PubMed:24210219};
GN Name=yceF; OrderedLocusNames=b1087, JW5155;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1447160; DOI=10.1128/jb.174.23.7873-7874.1992;
RA Oh W., Larson T.J.;
RT "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the
RT Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 174:7873-7874(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5] {ECO:0007744|PDB:4JHC}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP TRP-12; ARG-13; LYS-52; ASP-69; GLN-70; LYS-81 AND GLU-154.
RX PubMed=24210219; DOI=10.1016/j.chembiol.2013.09.011;
RA Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X.,
RA Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N.,
RA Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G.,
RA Yakunin A.F.;
RT "Biochemical and structural studies of conserved Maf proteins revealed
RT nucleotide pyrophosphatases with a preference for modified nucleotides.";
RL Chem. Biol. 20:1386-1398(2013).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-
CC methyl-GTP (m(7)GTP) (PubMed:24210219). May have a dual role in cell
CC division arrest and in preventing the incorporation of modified
CC nucleotides into cellular nucleic acids (PubMed:24210219).
CC {ECO:0000269|PubMed:24210219}.
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 ECO:0000269|PubMed:24210219};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32.8 uM for m(7)GTP {ECO:0000269|PubMed:24210219};
CC Note=kcat is 1.2 sec(-1). {ECO:0000269|PubMed:24210219};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:24210219}.
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, ECO:0000305|PubMed:24210219}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23829.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M96791; AAA23829.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74171.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35895.2; -; Genomic_DNA.
DR PIR; D64852; D64852.
DR RefSeq; NP_415605.2; NC_000913.3.
DR RefSeq; WP_001125202.1; NZ_SSZK01000019.1.
DR PDB; 4JHC; X-ray; 1.85 A; A/B=1-194.
DR PDBsum; 4JHC; -.
DR AlphaFoldDB; P0A729; -.
DR SMR; P0A729; -.
DR BioGRID; 4261026; 139.
DR DIP; DIP-48156N; -.
DR STRING; 511145.b1087; -.
DR jPOST; P0A729; -.
DR PaxDb; P0A729; -.
DR PRIDE; P0A729; -.
DR EnsemblBacteria; AAC74171; AAC74171; b1087.
DR EnsemblBacteria; BAA35895; BAA35895; BAA35895.
DR GeneID; 66670647; -.
DR GeneID; 945631; -.
DR KEGG; ecj:JW5155; -.
DR KEGG; eco:b1087; -.
DR PATRIC; fig|511145.12.peg.1130; -.
DR EchoBASE; EB1408; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_0_6; -.
DR InParanoid; P0A729; -.
DR OMA; CAGSFKA; -.
DR PhylomeDB; P0A729; -.
DR BioCyc; EcoCyc:EG11438-MON; -.
DR BioCyc; MetaCyc:EG11438-MON; -.
DR PRO; PR:P0A729; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..194
FT /note="7-methyl-GTP pyrophosphatase"
FT /id="PRO_0000122975"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 12
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 70
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 154
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT MUTAGEN 12
FT /note="W->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 12
FT /note="W->R: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 13
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 52
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 69
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 70
FT /note="Q->A,T: No change in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 81
FT /note="K->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 154
FT /note="E->A,Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:4JHC"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:4JHC"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:4JHC"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4JHC"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:4JHC"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:4JHC"
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
