ID   DER_VIBC3               Reviewed;         494 AA.
AC   A5F3E6; C3LYD1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN   OrderedLocusNames=VC0395_A0292, VC395_0780;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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; CP000627; ABQ21537.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08797.1; -; Genomic_DNA.
DR   RefSeq; WP_000249403.1; NZ_JAACZH010000017.1.
DR   AlphaFoldDB; A5F3E6; -.
DR   SMR; A5F3E6; -.
DR   STRING; 345073.VC395_0780; -.
DR   PRIDE; A5F3E6; -.
DR   EnsemblBacteria; ABQ21537; ABQ21537; VC0395_A0292.
DR   GeneID; 57739473; -.
DR   KEGG; vco:VC0395_A0292; -.
DR   KEGG; vcr:VC395_0780; -.
DR   PATRIC; fig|345073.21.peg.754; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_5_1_6; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..494
FT                   /note="GTPase Der"
FT                   /id="PRO_1000071709"
FT   DOMAIN          3..166
FT                   /note="EngA-type G 1"
FT   DOMAIN          206..379
FT                   /note="EngA-type G 2"
FT   DOMAIN          380..464
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         212..219
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         259..263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         324..327
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   494 AA;  55638 MW;  A6F0020F23CE7645 CRC64;
     MVPVVALVGR PNVGKSTLFN RLTRTRDALV ADFPGLTRDR KYGQAKLGEH EFIVIDTGGI
     DGSEEGVETK MAQQSLAAID EADVVLFMVD GRAGLTVADE AIAQHLRRIE KPAILVVNKV
     DGIDADAASA EFWQLGMDQM YQIAAAHGRG VGALIDRVLN PFAEQMESEQ AQLEDLTNEE
     DPEEEQLEYS EEEAEAEYKR LQDLPIKLAI IGRPNVGKST LTNRILGEER VVVYDMPGTT
     RDSIYIPMKR DEREYVLIDT AGVRRRKRIN ETVEKFSVVK TLQAIEDANV VLLVVDAREN
     ISDQDLSLLG FALNSGRSIV IAVNKWDGLS FDVKEHVKKE LDRRLGFVDF ARIHFISALH
     GTGVGHLFES VQEAYRSATT RVGTSVLTRI MKMATDDHQP PMVRGRRVKL KYAHAGGYNP
     PIIVIHGNQV NELPDSYKRY LMNYYRKSLE IMGTPIRIQF QNSENPFEGK TNKMTLSQER
     QRKRLMSMVK NRRK