ID   DER_NEIG1               Reviewed;         485 AA.
AC   O87407; Q5F9H0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=GTPase Der;
DE   AltName: Full=GTP-binding protein EngA;
GN   Name=der; Synonyms=engA; OrderedLocusNames=NGO0424;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=10655208; DOI=10.1093/genetics/154.2.523;
RA   Mehr I.J., Long C.D., Serkin C.D., Seifert H.S.;
RT   "A homologue of the recombination-dependent growth gene, rdgC, is involved
RT   in gonococcal pilin antigenic variation.";
RL   Genetics 154:523-532(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Essential. {ECO:0000269|PubMed:10655208}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family. {ECO:0000305}.
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DR   EMBL; AF058711; AAC63508.1; -; Genomic_DNA.
DR   EMBL; AE004969; AAW89167.1; -; Genomic_DNA.
DR   RefSeq; WP_010951041.1; NC_002946.2.
DR   RefSeq; YP_207579.1; NC_002946.2.
DR   AlphaFoldDB; O87407; -.
DR   SMR; O87407; -.
DR   STRING; 242231.NGO_0424; -.
DR   PRIDE; O87407; -.
DR   EnsemblBacteria; AAW89167; AAW89167; NGO_0424.
DR   KEGG; ngo:NGO_0424; -.
DR   PATRIC; fig|242231.10.peg.508; -.
DR   HOGENOM; CLU_016077_6_2_4; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000000535; 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..485
FT                   /note="GTPase Der"
FT                   /id="PRO_0000179019"
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   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"
FT   BINDING         56..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         182..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   485 AA;  54028 MW;  19161A08B63857FC CRC64;
     MKPTIALIGR PNVGKSTLFN RLTRTKDALV HDLPGLTRDR HYGHGKVGSK PYFVIDTGGF
     EPVVDSGILH EMAKQTLQAV DEADAVVFLV DGRTGLTPQD KIIADRLRQS PRPVYLAVNK
     GEGGDRAVLA AEFYELALGE PHVISGAHGD GVYYLIEEIL ENFPEPEAEE ADAKHPVFAV
     IGRPNVGKST LVNAILGEKR VIAFDMAGTT RDSIHIDFER EGKPFTIIDT AGVRRRGKVD
     EAVEKFSVIK AMQAVEAANV AVLVLDAQQD IADQDATIAG FALEAGRALV VAVNKWDGIS
     EERREQVKRD ISRKLYFLDF AKFHFISALK ERGIDGLFES IQAAYNAAMI KMPTPKITRV
     LQTAVERQQP PRAGLVRPKM RYAHQGGMNP PVIVVHGNSL HAISDSYTRY LTQTFRKAFN
     LQGTPLRIQY NVSENPYENA EDKPKKKPLR RVSLSNRIEK REGRKEEKNR FKKKTKVSVK
     KQFSK