MNME_CHLTE
ID MNME_CHLTE Reviewed; 473 AA.
AC Q8KAS1;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=CT2084;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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 -!- INTERACTION:
CC Q8KAS1; Q8KAS1: mnmE; NbExp=2; IntAct=EBI-15807975, EBI-15807975;
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; AE006470; AAM73301.1; -; Genomic_DNA.
DR RefSeq; NP_662959.1; NC_002932.3.
DR RefSeq; WP_010933739.1; NC_002932.3.
DR PDB; 3GEE; X-ray; 2.95 A; A=1-473.
DR PDB; 3GEI; X-ray; 3.40 A; A/B/C=1-473.
DR PDBsum; 3GEE; -.
DR PDBsum; 3GEI; -.
DR AlphaFoldDB; Q8KAS1; -.
DR SMR; Q8KAS1; -.
DR DIP; DIP-48420N; -.
DR STRING; 194439.CT2084; -.
DR EnsemblBacteria; AAM73301; AAM73301; CT2084.
DR KEGG; cte:CT2084; -.
DR PATRIC; fig|194439.7.peg.1887; -.
DR eggNOG; COG0486; Bacteria.
DR HOGENOM; CLU_019624_4_1_10; -.
DR OMA; CEIQCHG; -.
DR OrthoDB; 263682at2; -.
DR EvolutionaryTrace; Q8KAS1; -.
DR Proteomes; UP000001007; 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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; tRNA processing.
FT CHAIN 1..473
FT /note="tRNA modification GTPase MnmE"
FT /id="PRO_0000188866"
FT DOMAIN 230..394
FT /note="TrmE-type G"
FT BINDING 31
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 95
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 134
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 240..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 259..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 284..287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 473
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 STRAND 15..18
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3GEE"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 200..229
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:3GEE"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3GEI"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:3GEE"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:3GEI"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3GEE"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:3GEE"
FT TURN 427..432
FT /evidence="ECO:0007829|PDB:3GEE"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 438..453
FT /evidence="ECO:0007829|PDB:3GEE"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:3GEE"
SQ SEQUENCE 473 AA; 51817 MW; B7F2E17B3A8793E2 CRC64;
MSPSDLHLPV PGHPIAAIAT PVGVGALAIV RISGAGVLDL ADRVFRKVHG SGKLAEAAGY
TAHFGRLYDG EEMVDEVIAL VFRAPRSFTA EQMVEFTCHG GPVVVGRVLR LMLDNGCRLA
EPGEFTRRAF LNGRIDLLQA EAIGEMIHAR TESAYRTAVS QMKGDLSVRL GGLREQLIRS
CALIELELDF SEEDVEFQSR DELTMQIETL RSEVNRLIDS YQHGRIVSEG VSTVIAGKPN
AGKSTLLNTL LGQERAIVSH MPGTTRDYIE ECFIHDKTMF RLTDTAGLRE AGEEIEHEGI
RRSRMKMAEA DLILYLLDLG TERLDDELTE IRELKAAHPA AKFLTVANKL DRAANADALI
RAIADGTGTE VIGISALNGD GIDTLKQHMG DLVKNLDKLH EASVLVTSLR HYEALRNASD
ALQNALELIA HESETELIAF ELRAALDYVG QITGKVVNEE VLNTIFDKFC IGK
