DER_RUEPO
ID DER_RUEPO Reviewed; 487 AA.
AC Q5LR04;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, 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=SPO2328;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV95590.1; -; Genomic_DNA.
DR RefSeq; WP_011048045.1; NC_003911.12.
DR AlphaFoldDB; Q5LR04; -.
DR SMR; Q5LR04; -.
DR STRING; 246200.SPO2328; -.
DR EnsemblBacteria; AAV95590; AAV95590; SPO2328.
DR KEGG; sil:SPO2328; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_5_0_5; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000001023; 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 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; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..487
FT /note="GTPase Der"
FT /id="PRO_1000011743"
FT DOMAIN 3..167
FT /note="EngA-type G 1"
FT DOMAIN 203..378
FT /note="EngA-type G 2"
FT DOMAIN 379..465
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT REGION 167..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..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 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 209..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 256..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 321..324
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; 53835 MW; A29D8EAA3A65FBAA CRC64;
MSLTLAIVGR PNVGKSTLFN RLVGKRLALV DDQPGVTRDL REGQARLGDL RFTVIDTAGL
ETATDDSLQG RMRRLTERAV DMADICLFMI DARAGVTPND EIFADILRRR SAHVILAANK
AEGAAADAGV IEAYGLGLGE PIRLSAEHGE GLNELYAVLM PLADEMEQQA EEQAPETDVD
LDPEDEDGEE VAAPHAITRE KPLQVAVVGR PNAGKSTLIN RILGEDRLLT GPEAGITRDA
ISLQIDWNDT PMRIFDTAGM RKKAKVQEKL EKLSVSDGLR AVKFAEVVVV LLDAAIPFEQ
QDLRIADLAE REGRAVVIAV NKWDVEENKQ DKLRELKESF ERLLPQLRGA PLVTVSAKTG
RGLERLHDAI LRAHEVWNRR IPTAALNRWL IGMLEQHPPP APQGKRIKLR YMTQAKTRPP
GFVVMCSHPD KMPESYSRYL VNGLRADFDM PGTPIRLTLR GQGDKNPYKG RRKKNAGALA
KHLKSRG
