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DER_STRP2
ID   DER_STRP2               Reviewed;         436 AA.
AC   Q04J64;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SPD_1519;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ54175.1; -; Genomic_DNA.
DR   RefSeq; WP_001207696.1; NC_008533.2.
DR   AlphaFoldDB; Q04J64; -.
DR   SMR; Q04J64; -.
DR   STRING; 373153.SPD_1519; -.
DR   EnsemblBacteria; ABJ54175; ABJ54175; SPD_1519.
DR   GeneID; 60233890; -.
DR   GeneID; 66806783; -.
DR   KEGG; spd:SPD_1519; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_9; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   BioCyc; SPNE373153:G1G6V-1641-MON; -.
DR   Proteomes; UP000001452; 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_1000011752"
FT   DOMAIN          4..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          175..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         181..188
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;  49082 MW;  B013890D5285BBED CRC64;
     MALPTIAIVG RPNVGKSTLF NRIAGERISI VEDVEGVTRD RIYATGEWLN RSFSMIDTGG
     IDDVDAPFME QIKHQAEIAM EEADVIVFVV SGKEGITDAD EYVARKLYKT HKPVILAVNK
     VDNPEMRNDI YDFYALGLGE PLPISSVHGI GTGDVLDAIV ENLPNEYEEE NPDVIKFSLI
     GRPNVGKSSL INAILGEDRV IASPVAGTTR DAIDTHFTDT DGQEFTMIDT AGMRKSGKVY
     ENTEKYSVMR AMRAIDRSDV VLMVINAEEG IREYDKRIAG FAHEAGKGMI IVVNKWDTLE
     KDNHTMKNWE EDIREQFQYL PYAPIIFVSA LTKQRLHKLP EMIKQISESQ NTRIPSAVLN
     DVIMDAIAIN PTPTDKGKRL KIFYATQVAT KPPTFVIFVN EEELMHFSYL RFLENQIRKA
     FVFEGTPIHL IARKRK
 
 
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