ID   DER_ALTMD               Reviewed;         481 AA.
AC   B4RV85; F2G259;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=der1 {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA1;
GN   OrderedLocusNames=MADE_1005235;
GN   and
GN   Name=der2 {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA2;
GN   OrderedLocusNames=MADE_1012830;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(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; CP001103; AEA97193.1; -; Genomic_DNA.
DR   EMBL; CP001103; AEA98700.1; -; Genomic_DNA.
DR   RefSeq; WP_012517547.1; NC_011138.3.
DR   AlphaFoldDB; B4RV85; -.
DR   SMR; B4RV85; -.
DR   EnsemblBacteria; AEA97193; AEA97193; MADE_1005235.
DR   GeneID; 56343082; -.
DR   KEGG; amc:MADE_1005235; -.
DR   HOGENOM; CLU_016077_6_2_6; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000001870; 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 2.
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..481
FT                   /note="GTPase Der"
FT                   /id="PRO_1000099088"
FT   DOMAIN          3..166
FT                   /note="EngA-type G 1"
FT   DOMAIN          194..367
FT                   /note="EngA-type G 2"
FT   DOMAIN          368..452
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         118..121
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   481 AA;  53903 MW;  90FEAF64319A04FB CRC64;
     MLPVVALVGR PNVGKSTLFN RLTNTRDALV ADYPGLTRDR KYGQAKFEKR QFIVVDTGGI
     TGDEEGIDAE MAQQSLLAIE EADVVLFLVD ARAGLLPADQ GIADHLRRIN KQIFVVANKV
     DGIDGDSESA EFYSLGLGAI KQIAAAHGRG VSQLLQDALK PLESDFPDME IIDEAPEEEE
     DAESQRQRLQ ELPIKLAIVG KPNVGKSTLT NRILGEERVV VYDMPGTTRD SVYIPMERDE
     REYILIDTAG VRKRKKISEA VEKFSIVKTL QAIEEANVVL LVIDAREGIT DQDLSLLGFV
     LNSGRSLVVA VNKWDGLSTD IKDDIKREMD RRLGFIDFAR IHFISALHGS GVGNLFESVQ
     EAYMSATKRI NTALLTQIME MAQDDHQPPL VRGRRVKMKY AHAGGYNPPV IVIHGNQVDD
     LPSSYKRFLM NYFRKALEIM GTPIKIEFRE GNNPFEGKKN NLTLAQQRKR RRMMSYYKEK
     K