DER_BRUME
ID DER_BRUME Reviewed; 483 AA.
AC Q8YFH2;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BMEI1550;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52731.1; -; Genomic_DNA.
DR PIR; AH3445; AH3445.
DR RefSeq; WP_004682999.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YFH2; -.
DR SMR; Q8YFH2; -.
DR STRING; 224914.BMEI1550; -.
DR EnsemblBacteria; AAL52731; AAL52731; BMEI1550.
DR GeneID; 29594398; -.
DR KEGG; bme:BMEI1550; -.
DR PATRIC; fig|224914.52.peg.2044; -.
DR eggNOG; COG1160; Bacteria.
DR OMA; KFRFLEY; -.
DR PhylomeDB; Q8YFH2; -.
DR Proteomes; UP000000419; Chromosome I.
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; 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 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Repeat; Ribosome biogenesis.
FT CHAIN 1..483
FT /note="GTPase Der"
FT /id="PRO_0000178972"
FT DOMAIN 3..167
FT /note="EngA-type G 1"
FT DOMAIN 212..387
FT /note="EngA-type G 2"
FT DOMAIN 388..472
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 218..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 265..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 330..333
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 483 AA; 53311 MW; 1624111DB29AA266 CRC64;
MGFTLAIVGR PNVGKSTLFN RLVGRKLALV DDLPGVTRDR RIHDAKLYDL KFQVIDTAGL
EEAANDSLEA RMRAQTEAAI SEADAVLFVI DAKAGITPAD STFAEAVRRS GKPVVLVANK
AEARGSEAGM YDAFQLGLGE PCPISAEHGQ GMPDLRDAIV ELLGEERVFA EERQEEAADE
VFTPAAVGAL VGDDIEDPDA EEIPAYDATK PLRIAIVGRP NAGKSTLINT MLGEDRLLTG
PEAGITRDSI SADWEWHGRK IKLFDTAGMR RKARVQEKLE KLSVADSLRA IRFAEVVIIV
LDATIPFEKQ DLQIADLIIR EGRAPVIAFN KWDLIEDRQM VLADLYEKTA RLLPQVRGLR
AVPISGERGQ GIDKLMENVV KTHEIWNRRI STGRLNRWLE GVIAHQPPPA VSGRRLKVKY
MTQVKTRPPG FVVSCSRPDA MPQSYVRYLI NGLRETFDMP GVPIRLSLRT SDNPFAGRAK
KKK
