DER_UREP2
ID DER_UREP2 Reviewed; 442 AA.
AC B1AJ22;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=UPA3_0399;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
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; CP000942; ACA33183.1; -; Genomic_DNA.
DR RefSeq; WP_006688696.1; NC_010503.1.
DR AlphaFoldDB; B1AJ22; -.
DR SMR; B1AJ22; -.
DR EnsemblBacteria; ACA33183; ACA33183; UPA3_0399.
DR GeneID; 29672164; -.
DR KEGG; upa:UPA3_0399; -.
DR HOGENOM; CLU_016077_6_2_14; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000002162; 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..442
FT /note="GTPase Der"
FT /id="PRO_1000077681"
FT DOMAIN 2..167
FT /note="EngA-type G 1"
FT DOMAIN 175..351
FT /note="EngA-type G 2"
FT DOMAIN 352..436
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 8..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 55..59
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 181..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 228..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 293..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 442 AA; 50547 MW; 11D7C67C92902932 CRC64;
MRTIAIVGKP NVGKSSLFNR ILMRRKSIVD DQPGVTRDRI YDIGNWLTRS FMLIDTGGII
SSKDTYQDNI NEQVLFAINE ANTIIFLVSA KDGINNDDKK IAKMLKEKAK DKKIILVINK
IESEKYYLNE GELYSFGFGK FFKISAEHGI GMGDLLDELV KDMPIQNNLE KQERFKFCII
GRPNVGKSSL TNTILGEQRV IVNAEAGSTR DSIDNDFNYY NKKYTIIDTA GIRRKGKIVE
SVEKYAVLRT KKAIERSQLI LLVLDGSEPF KEQDEVVGGL AYNANIPTII IVNKWDNIIN
KNSHTMEMVK KQIRSQFKYL SWAPIVFVSA LDNKRIHTIF EAIEFVREQA MRKIATSLLN
DVVIKANAFQ EPPPFKGGRI SISYIVQVQS QIPTFVLKCN NPKFLHFSYA RYIENEIRKA
FGFDSVPITL YWQDKNKKLR GE
