MNME_NEIMA
ID MNME_NEIMA Reviewed; 448 AA.
AC Q9JWB7; A1IPR7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379};
GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN Synonyms=thdF {ECO:0000255|HAMAP-Rule:MF_00379},
GN trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=NMA0454;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
CC -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate.
CC Involved in the addition of a carboxymethylaminomethyl (cmnm) group at
CC the wobble position (U34) of certain tRNAs, forming tRNA-
CC cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00379};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00379};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00379}.
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DR EMBL; AL157959; CAM07738.1; -; Genomic_DNA.
DR PIR; G81962; G81962.
DR RefSeq; WP_002246489.1; NC_003116.1.
DR AlphaFoldDB; Q9JWB7; -.
DR SMR; Q9JWB7; -.
DR EnsemblBacteria; CAM07738; CAM07738; NMA0454.
DR KEGG; nma:NMA0454; -.
DR HOGENOM; CLU_019624_4_1_4; -.
DR OMA; CEIQCHG; -.
DR BioCyc; NMEN122587:NMA_RS02305-MON; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; tRNA processing.
FT CHAIN 1..448
FT /note="tRNA modification GTPase MnmE"
FT /id="PRO_0000188894"
FT DOMAIN 216..373
FT /note="TrmE-type G"
FT BINDING 24
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 81
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 120
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 226..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 226
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 245..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 245
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 448
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
SQ SEQUENCE 448 AA; 47604 MW; 11DA91138052E875 CRC64;
MSDNVPTIAA VATAPGRGGV GVIRISGKNL LPMAQALCGK TPKPRVATYA DFTDEDGQAI
DSGLLLFFAA PASFTGEDVI ELQGHGGPVV MDMLLNRCLE LGARLAEPGE FTKRAFLNDK
LDLAQAEGVA DLIDASSRSA ARLALRSLKG DFSRRIHGLV EDLITLRMLV EATLDFPEED
IDFLEAADAR GKLDGLRRAV DDVLANAQQG AILREGLNVV LVGAPNVGKS SLLNALAGDE
VAIVTDIAGT TRDAVRERIL IDGVPVHIVD TAGLRETDDV VERIGIERSR KAVSEADVAL
VLVDPREGLN EKTRAILDAL PLELKRIEIH SKSDLHAHAA GGFGTGAETV IALSAKTGDG
LDALKRTLLR EAGWQGESEG LFLARTRHVN ALKAAQEELS LAALCGNHQI ELFAEHLRLA
QVACGEITGE FTADDLLGVI FSRFCIGK
