DER_CUPMC
ID DER_CUPMC Reviewed; 447 AA.
AC Q1LLJ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN OrderedLocusNames=Rmet_2102;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
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DR EMBL; CP000352; ABF08981.1; -; Genomic_DNA.
DR RefSeq; WP_011516815.1; NC_007973.1.
DR AlphaFoldDB; Q1LLJ5; -.
DR SMR; Q1LLJ5; -.
DR STRING; 266264.Rmet_2102; -.
DR EnsemblBacteria; ABF08981; ABF08981; Rmet_2102.
DR KEGG; rme:Rmet_2102; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_4; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 2.
DR PROSITE; PS51712; G_ENGA; 2.
PE 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..447
FT /note="GTPase Der"
FT /id="PRO_1000011712"
FT DOMAIN 3..167
FT /note="EngA-type G 1"
FT DOMAIN 181..354
FT /note="EngA-type G 2"
FT DOMAIN 355..439
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 9..16
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 56..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 187..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 234..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 299..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 447 AA; 49323 MW; AFADFA1EC0EDA542 CRC64;
MKPVIALVGR PNVGKSTLFN RMTRSRDALV ADLPGLTRDR HYGEGRIGDR PFIVIDTGGF
EPVAKEGIVA EMAKQTRQAV VEADVVIFLV DGRLGLAPQD RVIADYLRKT GRRVMLAINK
AEGMKYTSVA ADFYELGMGD PYAISSTHGD GVRELVDEAL DLAVQERPEL ADQEDAGQHG
VKIAIVGRPN VGKSTLVNTL IGEERVIAFD MPGTTRDAIY VEFERGGKPY TLIDTAGLRK
RGKVFEAIEK FSVVKTLQSI ADANVVVLLL DAQQDISEQD AHIAGFIVES GRALVVGVNK
WDGLDGHQRD RVKHDLERKL QFLSFANIHF VSARERTGIG ALLRSVDDAY AAAMIKLPTP
QITRVLQEAV EFQQPKRVGV SRPKLRYAHQ GGSNPPIIVV HGNALSGVTD AYRRYLENRF
RTAFKLKGTP LRIEFRTNKN PYAESKD
