ID   DER_BORAP               Reviewed;         433 AA.
AC   Q0SMZ9; G0ISF1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BAPKO_0536, BafPKo_0524;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01779.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69732.1; -; Genomic_DNA.
DR   RefSeq; WP_011601058.1; NC_017238.1.
DR   AlphaFoldDB; Q0SMZ9; -.
DR   SMR; Q0SMZ9; -.
DR   STRING; 390236.BafPKo_0524; -.
DR   EnsemblBacteria; AEL69732; AEL69732; BafPKo_0524.
DR   KEGG; baf:BAPKO_0536; -.
DR   KEGG; bafz:BafPKo_0524; -.
DR   PATRIC; fig|390236.22.peg.505; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_1_12; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   Proteomes; UP000005216; 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..433
FT                   /note="GTPase Der"
FT                   /id="PRO_1000011571"
FT   DOMAIN          5..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          174..349
FT                   /note="EngA-type G 2"
FT   DOMAIN          350..429
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         58..62
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         180..187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         227..231
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         292..295
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   433 AA;  49860 MW;  10ACA4551A52E98B CRC64;
     MLSYKKVLIV GRPNVGKSAL FNRILDTKRS ITENTYGVTR DLVEEVCKVG SFKFKLIDTG
     GFTILKDEIS KIVVQKVLSS LEKVDLILLV LDVNEILLED YQIIERLRKY SNKVILVLNK
     VDAKDKEFLA HEFHNLGFKR CFLVSAVHCR GIAKLRDFLK VEVGEANIED EVNIKVGIIG
     KPNSGKSTLI NYLSGNEISI VSDKPGTTRD FIKTKLTRNG KVFEIIDTAG IRRRARVNEI
     VEYYSVNRAL KVIDMVDIVF LLIDVKEELT SQDKKIAHYV TKKGKGIIIV FSKWDLVKES
     KGYFEALKSR VKFFFPVLNF APIFRISVHK KIGLDSLFKE AFKLKDQLEF KTSTPDLNKM
     LNLWIKDYHL NVSHKIKYIT QVSANPVRFI LFANKIKNFP NSYYNYLVNN LRKIGYNNIP
     ILVELREKIR DLK