ID MNME_RICTY Reviewed; 445 AA. AC Q68VZ0; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 112. 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=trmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN OrderedLocusNames=RT0745; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=257363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., RA Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with sequences RT of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017197; AAU04202.1; -; Genomic_DNA. DR RefSeq; WP_011191178.1; NC_006142.1. DR AlphaFoldDB; Q68VZ0; -. DR SMR; Q68VZ0; -. DR KEGG; rty:RT0745; -. DR eggNOG; COG0486; Bacteria. DR HOGENOM; CLU_019624_3_1_5; -. DR OrthoDB; 9805918at2; -. DR Proteomes; UP000000604; 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; IPR008144; Guanylate_kin-like_dom. 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; GTP-binding; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; tRNA processing. FT CHAIN 1..445 FT /note="tRNA modification GTPase MnmE" FT /id="PRO_0000278005" FT DOMAIN 215..371 FT /note="TrmE-type G" FT BINDING 20 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 79 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 119 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 225..230 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 225 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 229 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 244..250 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 244 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 246 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 249 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 250 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 269..272 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379" FT BINDING 445 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 445 AA; 49892 MW; 3E700EAC12F31B55 CRC64; METIFAQSSA FGKAGVAVFR ISGPKSLEVL QLLTGRKDFK PRLMYYQQII SPETNELIDN AMVVYFKLPN SFTGEDVVEI HTHGSKAISI MLINTLLNID DIRLAEAGEF TKRAFLNNKF DLTAAEGIAD LINAETIMQH RQAVRQANGG LEELYNNWRN QLLKIIALLE AYLDFPDEDI PDSILNDVNN THKNIVNEIS NYLNDNRRGE LLNNGLKLAI IGPPNTGKSS LLNFLMQRNI AIVSNIAGTT RDIIEGHLDI GGYPIILQDT AGIRAESTDI IEREGIKRAI NSAKTANIKI IMFDAEKLDL SINNDIIDLI DENTIVIINK IDLIEPSQIF PIEKKYKCLR VSVKNNIALS SILKNIENIA ENIAGFTETP YITNQRHRHY LKQALSHLMA FNLDNDLVLA TEDMRMTARC IGLITGVINV EEILNEIFKN FCIGK //