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DER_NEIMA
ID   DER_NEIMA               Reviewed;         485 AA.
AC   Q9JV01; A1IR91;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=NMA1063;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08277.1; -; Genomic_DNA.
DR   PIR; E81871; E81871.
DR   RefSeq; WP_002236872.1; NC_003116.1.
DR   AlphaFoldDB; Q9JV01; -.
DR   SMR; Q9JV01; -.
DR   EnsemblBacteria; CAM08277; CAM08277; NMA1063.
DR   KEGG; nma:NMA1063; -.
DR   HOGENOM; CLU_016077_6_2_4; -.
DR   OMA; KFRFLEY; -.
DR   BioCyc; NMEN122587:NMA_RS05315-MON; -.
DR   Proteomes; UP000000626; 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; Repeat; Ribosome biogenesis.
FT   CHAIN           1..485
FT                   /note="GTPase Der"
FT                   /id="PRO_0000179020"
FT   DOMAIN          3..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          176..349
FT                   /note="EngA-type G 2"
FT   DOMAIN          350..434
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   REGION          435..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..473
FT                   /note="Basic and acidic 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         182..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   485 AA;  54093 MW;  86DFE558C8BEC762 CRC64;
     MKPTIALVGR PNVGKSTLFN RLTRTKDALV HDLPGLTRDR HYGHGKVGSK PYLVIDTGGF
     EPVVDSGILH EMAKQTLQAV DEADAVVFLV DGRTGLTPQD KIIADRLRQS PRPVYLAVNK
     GEGGNRAVLA AEFYELALGD PYVISGAHGD GVYYLIEDIL ETFPEPEKEE EEAKHPVFAV
     IGRPNVGKST LVNAILGEER VIAFDMAGTT RDSIHIDFER EGKPFTIIDT AGVRRRGKVD
     EAVEKFSVIK AMQAVEAANV AVLVLDAQQD IADQDATIAG FALEAGRALV VAVNKWDGIS
     EERREQVKRD INRKLYFLDF AKFHFISALK ERGIDGLFDS IQAAYNAAMI KMPTPKITRV
     LQSAIERQQP PRAGLVRPKM RYAHQGGMNP PVIVVHGNSL HAISDSYTRY LTQTFRKAFN
     LQGTPLRIQY NVSENPYENA DDKPKKKPLR RVSLSNRIEK REGRKEEKNR FKKKTKVSVK
     KQFSK
 
 
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