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Database: UniProt
Entry: A0A378I5D6_9GAMM
LinkDB: A0A378I5D6_9GAMM
Original site: A0A378I5D6_9GAMM 
ID   A0A378I5D6_9GAMM        Unreviewed;       448 AA.
AC   A0A378I5D6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=tRNA modification GTPase MnmE {ECO:0000256|HAMAP-Rule:MF_00379};
DE            EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_00379};
GN   Name=mnmE {ECO:0000256|HAMAP-Rule:MF_00379,
GN   ECO:0000313|EMBL:STX30243.1};
GN   Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN   ORFNames=NCTC13315_02808 {ECO:0000313|EMBL:STX30243.1};
OS   Legionella beliardensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=91822 {ECO:0000313|EMBL:STX30243.1, ECO:0000313|Proteomes:UP000254968};
RN   [1] {ECO:0000313|EMBL:STX30243.1, ECO:0000313|Proteomes:UP000254968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13315 {ECO:0000313|EMBL:STX30243.1,
RC   ECO:0000313|Proteomes:UP000254968};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00379}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00379};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00379};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00379}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00379}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. TrmE GTPase family. {ECO:0000256|ARBA:ARBA00011043,
CC       ECO:0000256|HAMAP-Rule:MF_00379, ECO:0000256|RuleBase:RU003313}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00379}.
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DR   EMBL; UGNV01000001; STX30243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A378I5D6; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000254968; Unassembled WGS sequence.
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   CDD; cd14858; TrmE_N; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.430; tRNA modification GTPase MnmE domain 2; 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   NCBIfam; TIGR00450; mnmE_trmE_thdF; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42714; TRNA MODIFICATION GTPASE GTPBP3; 1.
DR   PANTHER; PTHR42714:SF2; TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF12631; MnmE_helical; 1.
DR   Pfam; PF10396; TrmE_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF116878; TrmE connector domain; 1.
DR   PROSITE; PS51709; G_TRME; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00379};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00379};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00379, ECO:0000313|EMBL:STX30243.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00379};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00379};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00379};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00379};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254968};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00379}.
FT   DOMAIN          217..372
FT                   /note="TrmE-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51709"
FT   BINDING         24
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         82
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         121
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         227..232
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         227
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         246..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         246
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         248
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         251
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         271..274
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00379"
SQ   SEQUENCE   448 AA;  49195 MW;  25867ED626D04FC4 CRC64;
     MSLAEETIVA IATPPGRGGV GIIRLSGPSA YLITKQLTKQ MDLTPRHAVY TAFFDKQNKL
     IDKGLVLYFK APHSFTGEDV IELQGHGAPV ILDYLVQECI AYGARLARPG EFSERAFLND
     KIDLAQAEAI ADLIHASSLT AARMAVRSLQ GDFSHKIAEL NEKIINLRLY VEAAIDFPEE
     EIDFLSDGKV AVQLTEIVNN LDILRQNATQ GVMLREGLTI VIAGEPNTGK STLINCLACR
     EVAIVTDIAG TTRDVMREYV LLDGLPVHLI DTAGLRESND IVEQEGIKRA WQEIRKADCV
     LLLADVQQKN QPNELDEAIL SSLPTGTPLL KVFNKIDTIN EKPKCEEDAI YLSAKSGAGI
     DLLLTKIKAL VGFHPTEGQF LARRRHLDAL DRAKEFLLTG QMQLINARAG ELLADDLRLA
     HQCLSEITGE FTPDDLLGKI FSSFCIGK
//
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