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Database: UniProt
Entry: A0A1P8FK39_9PROT
LinkDB: A0A1P8FK39_9PROT
Original site: A0A1P8FK39_9PROT 
ID   A0A1P8FK39_9PROT        Unreviewed;       467 AA.
AC   A0A1P8FK39;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=GTPase Der {ECO:0000256|ARBA:ARBA00020953, ECO:0000256|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000256|HAMAP-Rule:MF_00195};
GN   ORFNames=BWI17_12735 {ECO:0000313|EMBL:APV50481.1};
OS   Betaproteobacteria bacterium GR16-43.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV50481.1, ECO:0000313|Proteomes:UP000185830};
RN   [1] {ECO:0000313|EMBL:APV50481.1, ECO:0000313|Proteomes:UP000185830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GR16-43 {ECO:0000313|EMBL:APV50481.1,
RC   ECO:0000313|Proteomes:UP000185830};
RA   Choi A.;
RT   "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT   freshwater pond in South Korea.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|RuleBase:RU004481}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|PROSITE-ProRule:PRU01049, ECO:0000256|RuleBase:RU004481}.
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DR   EMBL; CP019169; APV50481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8FK39; -.
DR   STRING; 1904640.BWI17_12735; -.
DR   KEGG; beba:BWI17_12735; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000185830; 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:SF6; GTP-BINDING PROTEIN ENGA; 1.
DR   PANTHER; PTHR43834; 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00195};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00195};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU004481};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_00195}.
FT   DOMAIN          3..168
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          177..350
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         9..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         56..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         183..190
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         230..234
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         295..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   467 AA;  51209 MW;  61979BB2824333E3 CRC64;
     MKPTVVLVGR PNVGKSTLFN RLTRSRDALV ADLPGLTRDR HYGQGRLGDK AFIVVDTGGF
     EPVAKEGILS EMARQAREAI AEADIIIFLV DGRAGLAPQD KRIAAMLRKE ASAPVFLAVN
     KTEGMREAIV TAEFHELALG DPIAISAEHG EGVRQMIEDA LAAFPEDEDE EEVPDHPRVA
     IVGRPNVGKS TLVNRLLGEE RVIAFDQPGT TRDAIEVELS WEGKRYTLID TAGIRKRGKV
     WEAVEKFSVV KTLQAIERAN VVILVVDADQ DIAEQDAHIG GYILEAGRAL VVAVNKVDAI
     DSEKRKDVAS DLERKLHFLD FAEFHSISAR HGTGIKKMLQ AVDGAFAAAM AKLSTPKLTR
     ALIAAVQEQQ PPLAGKIRPK LRYAHQGGMN PPIVVIHGTS TASIKATYKR YLEGVFIRTF
     KLKGTPLRVE LRSGVNPYAG KKAQVLTVSQ ERAKRKNRIY SKRKYGN
//
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