DER_BACC3
ID DER_BACC3 Reviewed; 436 AA.
AC C1EN01;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=BCA_1563;
OS Bacillus cereus (strain 03BB102).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=572264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03BB102;
RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA Tapia R., Han C., Sutton G., Sims D.;
RT "Genome sequence of Bacillus cereus 03BB102.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001407; ACO28532.1; -; Genomic_DNA.
DR RefSeq; WP_001125893.1; NZ_CP009318.1.
DR AlphaFoldDB; C1EN01; -.
DR SMR; C1EN01; -.
DR EnsemblBacteria; ACO28532; ACO28532; BCA_1563.
DR GeneID; 64203052; -.
DR GeneID; 67506206; -.
DR KEGG; bcx:BCA_1563; -.
DR PATRIC; fig|572264.18.peg.1511; -.
DR OMA; KFRFLEY; -.
DR Proteomes; UP000002210; 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; 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..436
FT /note="GTPase Der"
FT /id="PRO_1000124341"
FT DOMAIN 4..167
FT /note="EngA-type G 1"
FT DOMAIN 176..351
FT /note="EngA-type G 2"
FT DOMAIN 352..436
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 57..61
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 182..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 229..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 294..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 436 AA; 48618 MW; 100BD130FEA7A3DD CRC64;
MPKPVIAIVG RPNVGKSTIF NRIVGERVSI VEDIPGVTRD RIYSAGEWLN HEFNIIDTGG
IDIGDEPFLT QIRQQAEVAI DEADVIIFMT NGRDGVTAAD EEVAKILYRS NKPVVLAVNK
VDNPEMRSDI YDFYALGFGE PFPISGTHGL GLGDLLDEAA QHFPKIEEDG YDEDTIRFSL
IGRPNVGKSS LVNALLGQER VIVSNVAGTT RDAVDTPYSK DGKDYVIIDT AGMRKKGKVY
ESTEKYSVLR ALRAIERSDV VLVVLDGEEG IIEQDKKIAG YAHDSGRAVV IVVNKWDAVK
KDEKTMKAFE ENIRAHFQFL EYAPIVFLSA KTRKRTQTLI PVIDEVNESH SIRIQTNVLN
DVIMDAVAMN PTPTHNGSRL KIFYATQVAV KPPTFVVFVN DPELLHFSYE RFLKNRLRES
FGFVGTPIHI IARARD