DER_THEMA
ID DER_THEMA Reviewed; 439 AA.
AC Q9X1F8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=GTPase Der;
DE Short=TmDer;
DE AltName: Full=GTP-binding protein EngA;
GN Name=der; Synonyms=engA; OrderedLocusNames=TM_1446;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=11387344; DOI=10.1074/jbc.m104455200;
RA Hwang J., Inouye M.;
RT "An essential GTPase, der, containing double GTP-binding domains from
RT Escherichia coli and Thermotoga maritima.";
RL J. Biol. Chem. 276:31415-31421(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GDP, GTPASE ACTIVITY,
RP GTP-BINDING, DOMAINS, AND MUTAGENESIS OF ASN-118 AND ASN-300.
RX PubMed=12467572; DOI=10.1016/s0969-2126(02)00905-x;
RA Robinson V.L., Hwang J., Fox E., Inouye M., Stock A.M.;
RT "Domain arrangement of Der, a switch protein containing two GTPase
RT domains.";
RL Structure 10:1649-1658(2002).
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis (By similarity). Has GTPase activity but no ATPase
CC activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and UTP compete for
CC GTP binding. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for GTP {ECO:0000269|PubMed:11387344};
CC Vmax=0.35 umol/min/ug enzyme {ECO:0000269|PubMed:11387344};
CC Note=At pH 7.5, 70 degrees Celsius, 5 mM MgCl(2) and 400 mM KCl.;
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000250}.
CC -!- DOMAIN: Each G (guanine nucleotide-binding) domain has activity on its
CC own; domain 1 is twice as active as domain 2. The G domains do not
CC interact, instead each contacts the C-terminal KH-like domain which
CC lies between them. {ECO:0000269|PubMed:12467572}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36514.1; -; Genomic_DNA.
DR PIR; B72253; B72253.
DR RefSeq; NP_229245.1; NC_000853.1.
DR RefSeq; WP_004081721.1; NZ_CP011107.1.
DR PDB; 1MKY; X-ray; 1.90 A; A=2-439.
DR PDBsum; 1MKY; -.
DR AlphaFoldDB; Q9X1F8; -.
DR SMR; Q9X1F8; -.
DR STRING; 243274.THEMA_07085; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR EnsemblBacteria; AAD36514; AAD36514; TM_1446.
DR KEGG; tma:TM1446; -.
DR eggNOG; COG1160; Bacteria.
DR InParanoid; Q9X1F8; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR BRENDA; 3.6.5.2; 6331.
DR EvolutionaryTrace; Q9X1F8; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTP-bd_EngA.
DR InterPro; IPR032859; KH_dom-like.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 2.
DR PROSITE; PS51712; G_ENGA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..439
FT /note="GTPase Der"
FT /id="PRO_0000179064"
FT DOMAIN 2..168
FT /note="EngA-type G 1"
FT DOMAIN 181..357
FT /note="EngA-type G 2"
FT DOMAIN 358..439
FT /note="KH-like"
FT BINDING 8..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 55..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT BINDING 336..337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT MUTAGEN 118
FT /note="N->D: 10% of GTPase activity remains."
FT /evidence="ECO:0000269|PubMed:12467572"
FT MUTAGEN 300
FT /note="N->D: Slight increase of GTPase activity."
FT /evidence="ECO:0000269|PubMed:12467572"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 362..373
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:1MKY"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1MKY"
FT HELIX 409..422
FT /evidence="ECO:0007829|PDB:1MKY"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:1MKY"
SQ SEQUENCE 439 AA; 50015 MW; 29CA321453249B58 CRC64;
MATVLIVGRP NVGKSTLFNK LVKKKKAIVE DEEGVTRDPV QDTVEWYGKT FKLVDTCGVF
DNPQDIISQK MKEVTLNMIR EADLVLFVVD GKRGITKEDE SLADFLRKST VDTILVANKA
ENLREFEREV KPELYSLGFG EPIPVSAEHN INLDTLLETI IKKLEEKGLD LESKPEITDA
IKVAIVGRPN VGKSTLFNAI LNKERALVSP IPGTTRDPVD DEVFIDGRKY VFVDTAGLRR
KSRVEPRTVE KYSNYRVVDS IEKADVVVIV LDATQGITRQ DQRIAGLVER RGRASVVVFN
KWDLVEHREK RYDEFTKLFR EKLYFIDYSP LIFTSADKGW NIDRVIDAIN LAYASYTTKV
PSSAINSALQ KVLAFTNLPR GLKIFFGLQV DIKPPTFLFF VNSIEKVKNP QKIFLRKLIR
DYVFPFEGSP IFLKFKRSR
