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DER_PSEPW
ID   DER_PSEPW               Reviewed;         487 AA.
AC   B1JDV4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=PputW619_4321;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA74801.1; -; Genomic_DNA.
DR   RefSeq; WP_012316132.1; NC_010501.1.
DR   AlphaFoldDB; B1JDV4; -.
DR   SMR; B1JDV4; -.
DR   STRING; 390235.PputW619_4321; -.
DR   EnsemblBacteria; ACA74801; ACA74801; PputW619_4321.
DR   KEGG; ppw:PputW619_4321; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_6; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
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..487
FT                   /note="GTPase Der"
FT                   /id="PRO_1000099151"
FT   DOMAIN          3..166
FT                   /note="EngA-type G 1"
FT   DOMAIN          193..366
FT                   /note="EngA-type G 2"
FT   DOMAIN          367..451
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   REGION          448..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Basic 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         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         199..206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         246..250
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         311..314
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   487 AA;  54349 MW;  4086429E728D3496 CRC64;
     MVPVIALVGR PNVGKSTMFN RLTKTRDAIV GDLSGLTRDR QYGDASWQGR SFILIDTGGI
     TGDEVGMDEK MAEQSLMAIE EADYVLFLVD ARAGMTAADQ MIAEHLRKRN KSAILVANKI
     DNIDADVARA EFSPLGMGNA IPVAGSQGRG INQLMESVLG HIPRDAEEEA LDQEVAEGEE
     AVRIPGPSEK DGIKIAIIGR PNVGKSTLVN RMLGEERVVV YDQPGTTRDS IYIPFERDNE
     KYTFIDTAGV RKRGKIHEEV EKFSVVKTLQ AIKDANVVIF VMDAREGVVD HDLNLLGFAL
     EAGRAIVIAL NKWDGMESGE RDYVKTELER RLFFVDFADI HFISALHGTG VGHLYKSVQA
     AFKSAVTRWP TSRLTQILED AVSEHQPPLV NGRRIKLRYA HLGGANPPLI VIHGNQTEKI
     PKSYSRYLEN TYRRVLKLVG TPIRIEYKGG ENPYEGKKNT LTDRQVNKKR RLMSHHKKAE
     KKRRDKR
 
 
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