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DER_POLSJ
ID   DER_POLSJ               Reviewed;         447 AA.
AC   Q12AC2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Bpro_2604;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE44520.1; -; Genomic_DNA.
DR   RefSeq; WP_011483518.1; NC_007948.1.
DR   AlphaFoldDB; Q12AC2; -.
DR   SMR; Q12AC2; -.
DR   STRING; 296591.Bpro_2604; -.
DR   EnsemblBacteria; ABE44520; ABE44520; Bpro_2604.
DR   KEGG; pol:Bpro_2604; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_4; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   Proteomes; UP000001983; 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; Reference proteome; Repeat;
KW   Ribosome biogenesis.
FT   CHAIN           1..447
FT                   /note="GTPase Der"
FT                   /id="PRO_1000011689"
FT   DOMAIN          3..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          180..353
FT                   /note="EngA-type G 2"
FT   DOMAIN          354..438
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         186..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         233..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         298..301
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;  49144 MW;  10D5BB6C8CCD2B61 CRC64;
     MKPVIALVGR PNVGKSTIFN RLTKTRDAIV ADFAGLTRDR HYGNGKLGSH EYIVIDTGGF
     EPDAASGIYK EMAKQTRQAV AEADVVIFVV DARAGISAQD HDIANFLRKL GKPTVLTANK
     AEGMTEGVQF SEFFELGLGE VLPVSASHGQ GMRSLVDLAL APLHLADPDE EAEPQDPSVI
     RLAVAGRPNV GKSTLINTWL GEERLVSFDL PGTTRDAISV PFERAGQKFE LIDTAGLRRK
     GKVFEAIEKF SVVKTLQAIE GANVVLLLLD ATQGVTDQDA HIAGYILESG RAVVLAINKW
     DAVDAYQRET LERSIETRLA FLKFASIHKI SAIKRQGLAP VWKSIVQAHA SANRKMSTPV
     LTRLLLEAVQ FQQPQRSGMF RPKMRYAHQG GMNPPIIIIH GNSLEHVTEA YKRYLEGRFR
     KEFDLVGTPM RIQMKSSHNP FTDKDSA
 
 
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