DER_CAMJJ
ID DER_CAMJJ Reviewed; 460 AA.
AC A1VYA6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, 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=CJJ81176_0409;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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; CP000538; EAQ73463.1; -; Genomic_DNA.
DR RefSeq; WP_002854274.1; NC_008787.1.
DR AlphaFoldDB; A1VYA6; -.
DR SMR; A1VYA6; -.
DR STRING; 354242.CJJ81176_0409; -.
DR EnsemblBacteria; EAQ73463; EAQ73463; CJJ81176_0409.
DR KEGG; cjj:CJJ81176_0409; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_7; -.
DR OMA; KFRFLEY; -.
DR Proteomes; UP000000646; 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..460
FT /note="GTPase Der"
FT /id="PRO_1000011595"
FT DOMAIN 2..164
FT /note="EngA-type G 1"
FT DOMAIN 196..368
FT /note="EngA-type G 2"
FT DOMAIN 369..453
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 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 202..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 249..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 313..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 460 AA; 52600 MW; 5F841D3E96BEBB31 CRC64;
MQSIILIGKP NVGKSSLFNR MARQRIAITS DISGTTRDTN KTQIHIHSKK AMLIDSGGLD
ESDELFKNVK KNTLKVAKES DIILYLVDGK LAPDDEDRQF FYSLKKLGKP IALVVNKVDN
KKDEERAWEF ANFGVKEIFN LSVTHNVGLD ELYEWLEKFL HEEFLIPDEE ENLEDFLEHY
EEGKEFQFKE VDQNHIRVGI VGRVNVGKSS LLNALVKQER SVVSSIAGTT IDPVNESVVH
KDKVIEFVDT AGIRKRGKIQ GLERFALNRT EKILSHSQIA LLVLDAHEGF NELDERIAGL
VAKHYLGVII VLNKWDKSEM DFDKTVKELR LDRFKFLAYA PVISVSALSG KRVHVLLDKI
LQIFENFTQK IQTSKLNTLI ENATRAHPLP HDYGKLVKIY YAVQYDLAPP KIALIMNRPK
ALHFSYKRYL QNQIRKEFNF EGVPLVIASR KKGSKENDES
