DER_MYCMM
ID DER_MYCMM Reviewed; 469 AA.
AC B2HRU9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=MMAR_2528;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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; CP000854; ACC40979.1; -; Genomic_DNA.
DR RefSeq; WP_012394265.1; NC_010612.1.
DR AlphaFoldDB; B2HRU9; -.
DR SMR; B2HRU9; -.
DR STRING; 216594.MMAR_2528; -.
DR EnsemblBacteria; ACC40979; ACC40979; MMAR_2528.
DR KEGG; mmi:MMAR_2528; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_11; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000001190; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 2.
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..469
FT /note="GTPase Der"
FT /id="PRO_1000099140"
FT DOMAIN 30..193
FT /note="EngA-type G 1"
FT DOMAIN 203..376
FT /note="EngA-type G 2"
FT DOMAIN 377..459
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 145..148
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 469 AA; 50871 MW; 2269E4541E1F09E4 CRC64;
MTQDGTWSDE SDWELDDADL ADLAEAAPAP VLAIVGRPNV GKSTLVNRIL GRREAVVQDI
PGVTRDRVSY DALWNGRRFV VQDTGGWEPD AKGLQQLVAE QASVAMRTAD AVVLVVDATV
GATTADEAAA RILLRSGKPV FLAANKVDSD KAEADAATLW SMGLGEPHAI SAMHGRGVAD
LLDTVLKKLP EVAESVSAGG GPRRVALVGK PNVGKSSLLN KLAGDERSVV HDVAGTTVDP
VDSLIELGGK VWRFVDTAGL RRKVGQASGH EFYASVRTRG AIDAAEVVVL LIDASQPLTE
QDLRVLSMVI EAGRAVVLAY NKWDLVDEDR RDLLDREIDR ELVQIRWAQR VNISAKTGRA
VQKLVPAMET ALASWDTRIP TGPLNSWIKE VVAATPPPVR GGKQPRILFA TQATARPPTF
VLFTTGFLEA GYRRFLERRL RETFGFEGSP IRINVRVREK RGAKRPGRR
