ID   DER_XANP2               Reviewed;         458 AA.
AC   A7IIE4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Xaut_2545;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) 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; CP000781; ABS67787.1; -; Genomic_DNA.
DR   RefSeq; WP_012114565.1; NC_009720.1.
DR   AlphaFoldDB; A7IIE4; -.
DR   SMR; A7IIE4; -.
DR   STRING; 78245.Xaut_2545; -.
DR   EnsemblBacteria; ABS67787; ABS67787; Xaut_2545.
DR   KEGG; xau:Xaut_2545; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_5_0_5; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   PhylomeDB; A7IIE4; -.
DR   Proteomes; UP000002417; 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   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..458
FT                   /note="GTPase Der"
FT                   /id="PRO_1000099180"
FT   DOMAIN          3..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          194..368
FT                   /note="EngA-type G 2"
FT   DOMAIN          369..453
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   REGION          167..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         200..207
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         247..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         312..315
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   458 AA;  49988 MW;  F79FC4B9F15C1A44 CRC64;
     MTFSLAIVGR PNVGKSTLFN RLVGKKLALV DDRPGVTRDR REGDARLGDL SFRIVDTAGL
     EEADAASLEG RMRAQTEAAI GHADAILFMI DARIGLTPTD RAFADLVRKC GKPVILLANK
     SEGRGGEAGT LEAFALGLGT PLPFSAEHGE GLSDLYDAIC DALPEQTRPE PEEDEDADTD
     FVEEEADDKP RRPIKVTVLG RPNAGKSTLI NRLLGEDRLL TGPEAGITRD SISVEVTYAG
     AKLEVFDTAG LRKRARIEDK LEKLSAADAL RAMKFAEVVV LLVDATHPFE EQDLRIADLV
     AREGRALVIG YNKSDLVARG GLITRLREDV DRLLPQVKGV PIVPVSGLMG HGLDKLVAAI
     SSAHKVWNKR VATNPLNRFL QQVTDNHPPP AVSGRRIKLR YMTQPKARPP SFVLFCSRTD
     AVPESYIRYL VNGLRETFDL PGVPIRLTLR EKGNPYAD