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Database: UniProt
Entry: S5LV80_9MOLU
LinkDB: S5LV80_9MOLU
Original site: S5LV80_9MOLU 
ID   S5LV80_9MOLU            Unreviewed;       450 AA.
AC   S5LV80;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379,
GN   ECO:0000313|EMBL:AGR41684.1};
GN   ORFNames=STAIW_v1c11010 {ECO:0000313|EMBL:AGR41684.1};
OS   Spiroplasma taiwanense CT-1.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR41684.1, ECO:0000313|Proteomes:UP000014984};
RN   [1] {ECO:0000313|EMBL:AGR41684.1, ECO:0000313|Proteomes:UP000014984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT-1 {ECO:0000313|EMBL:AGR41684.1};
RX   PubMed=23873917; DOI=10.1093/gbe/evt108;
RA   Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT   "Comparison of metabolic capacities and inference of gene content evolution
RT   in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL   Genome Biol. Evol. 5:1512-1523(2013).
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; CP005074; AGR41684.1; -; Genomic_DNA.
DR   RefSeq; WP_020834823.1; NC_021846.1.
DR   AlphaFoldDB; S5LV80; -.
DR   STRING; 1276220.STAIW_v1c11010; -.
DR   KEGG; stai:STAIW_v1c11010; -.
DR   PATRIC; fig|1276220.3.peg.1118; -.
DR   eggNOG; COG0486; Bacteria.
DR   HOGENOM; CLU_019624_4_1_14; -.
DR   Proteomes; UP000014984; 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   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; SSF103025; Folate-binding domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00379};
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:UP000014984};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00379}.
FT   DOMAIN          218..370
FT                   /note="TrmE-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51709"
FT   BINDING         25
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         228..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         228
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         247..253
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         247
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         249
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         252
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         272..275
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         450
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   450 AA;  50931 MW;  A445D3B7E99392CB CRC64;
     MKIDLDDVIV ACATKISKQA ISIVRLSGDD SIKIVNKILK KDLELKNKFQ LRKIYDKNNL
     IDESLILTFI GNKSFTGQTV VEINCHGGIL LTNKIISLLI ENGARLAKPG EFSQRAYLNG
     KINLLQAEGI NNLIESKNEL SLKINALNLE GSSNKKILDL KEKIIDLISK IQTSIDYPDY
     DDIEGASIQE IKISLKKIEN IIFKTIEISK RINTINHGIK TLILGETNVG KSSLLNSLLN
     DEKAIVTDIE GTTRDIVEGT INFENFTLDL IDSAGIRETN DIVEKIGVKK TISLINNSEL
     IFFIINYDKI NMELYDLIKE KKHIVVLNKV ETLSTSQINE VEKKFKDIVK ISALTNNIEE
     LLTKIEKDFN DSELLENDLP MLTNLYHIEQ FKEIFNLIRI SLENLEAGFS SELINIELYE
     ILKIINNLLG IFDADDEVID NIFRKYCLGK
//
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