DER_BACC2
ID DER_BACC2 Reviewed; 436 AA.
AC B7IP82;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=BCG9842_B3785;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) 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; CP001186; ACK98237.1; -; Genomic_DNA.
DR RefSeq; WP_001125890.1; NC_011772.1.
DR AlphaFoldDB; B7IP82; -.
DR SMR; B7IP82; -.
DR EnsemblBacteria; ACK98237; ACK98237; BCG9842_B3785.
DR GeneID; 67465983; -.
DR KEGG; bcg:BCG9842_B3785; -.
DR HOGENOM; CLU_016077_6_2_9; -.
DR OMA; KFRFLEY; -.
DR Proteomes; UP000006744; 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_1000118636"
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; 48726 MW; 3AA7E0FEFA6455C2 CRC64;
MPKPVIAIVG RPNVGKSTIF NRIVGERVSI VEDIPGITRD RIYSAGEWLN HEFNIIDTGG
IDIGDEPFLT QIRQQAEVAI DEADVIIFMT NGRDGVTAAD EEVAKILYRS KKPIVLAVNK
VDNPEMRSDI YDFYSLGFGE PFPISGTHGL GLGDLLDEAA NHFPKIEEEA YDDETIRFSL
IGRPNVGKSS LVNALLGQER VIVSNIAGTT RDAVDTPYSK DDQDYVIIDT AGMRKKGKVY
ESTEKYSVLR ALRAIERSDV VLVVLDGEEG IIEQDKKIAG YAHDSGRAVI IVVNKWDAVK
KDEKTMKAFE ENIRAHFQFL DYAPIVFLSA KTKKRTQTLL PVINEVNESH SIRVQTNVLN
DVIMDAVAMN PTPTHNGSRL KIFYATQVAV KPPTFVVFVN DTELMHFSYE RFLKNRLREA
FGFVGTPIHI IARARD