ID DER_BORPE Reviewed; 451 AA. AC Q7VWL4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 110. 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=BP2195; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX640417; CAE42473.1; -; Genomic_DNA. DR RefSeq; NP_880843.1; NC_002929.2. DR RefSeq; WP_003810703.1; NZ_CP039022.1. DR AlphaFoldDB; Q7VWL4; -. DR SMR; Q7VWL4; -. DR STRING; 257313.BP2195; -. DR PaxDb; 257313-BP2195; -. DR GeneID; 69601971; -. DR KEGG; bpe:BP2195; -. DR PATRIC; fig|257313.5.peg.2369; -. DR eggNOG; COG1160; Bacteria. DR HOGENOM; CLU_016077_5_0_4; -. DR Proteomes; UP000002676; Chromosome. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR CDD; cd01894; EngA1; 1. DR CDD; cd01895; EngA2; 1. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTPase_Der. 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 NCBIfam; TIGR03594; GTPase_EngA; 1. DR NCBIfam; TIGR00231; small_GTP; 2. DR PANTHER; PTHR43834; GTPASE DER; 1. DR PANTHER; PTHR43834:SF6; GTPASE DER; 1. 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; P-loop containing nucleoside triphosphate hydrolases; 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..451 FT /note="GTPase Der" FT /id="PRO_0000178970" FT DOMAIN 5..170 FT /note="EngA-type G 1" FT DOMAIN 186..359 FT /note="EngA-type G 2" FT DOMAIN 360..444 FT /note="KH-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 11..18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 58..62 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 192..199 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 239..243 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" FT BINDING 304..307 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195" SQ SEQUENCE 451 AA; 49428 MW; 2275B51A179C57FB CRC64; MSFKPVVALV GRPNVGKSTL FNRLTRSRAA LVADFSGLTR DRHYGEGRVG DTPFLVIDTG GFEPVAKDGI LAEMARQTRQ AIAEADVVVF LVDARAGVNA HDHEIARLLR KSGQQRVLLA VNKAEGMGVG NATGDFHELG LGEPHPISAA HGDGIVDLIE IALSGLVAPP ADTGEQLEQD VVDHRIKLAI VGRPNVGKST LINTLLGEER VIAFDMPGTT RDAIEIDFER DGRKYTLIDT AGLRKRGKVF EAIEKFSVIK TLQAIEASNV VLLMIDAQAE VSEQDAHIAG FVLETGRAVV VAINKWDGLD SDQRERIERE FQRKLRFLGF ARMHTISALK GQGVKPLLKS VNAAHAAAFA KLSTPRLTRE LQAAVEQQPP PRKGIFRPKM RYAHQGGQNP PLIVIHGNAL DAVPDSYRRY LETRFRNAFD LAGTPLRIEF KSSRNPYVQE N //