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Database: UniProt
Entry: G8LS15_9FLAO
LinkDB: G8LS15_9FLAO
Original site: G8LS15_9FLAO 
ID   G8LS15_9FLAO            Unreviewed;       441 AA.
AC   G8LS15;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=BLBCPU_345 {ECO:0000313|EMBL:AEU09388.1};
OS   Blattabacterium sp. (Cryptocercus punctulatus) str. Cpu.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1075399 {ECO:0000313|EMBL:AEU09388.1, ECO:0000313|Proteomes:UP000007112};
RN   [1] {ECO:0000313|EMBL:AEU09388.1, ECO:0000313|Proteomes:UP000007112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cpu {ECO:0000313|EMBL:AEU09388.1,
RC   ECO:0000313|Proteomes:UP000007112};
RX   PubMed=22094859;
RA   Neef A., Latorre A., Pereto J., Silva F.J., Pignatelli M., Moya A.;
RT   "Genome economization in the endosymbiont of the wood roach Cryptocercus
RT   punctulatus due to drastic loss of amino acid synthesis capabilities.";
RL   Genome Biol. Evol. 3:1437-1448(2011).
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; CP003015; AEU09388.1; -; Genomic_DNA.
DR   RefSeq; WP_014246276.1; NC_016621.1.
DR   AlphaFoldDB; G8LS15; -.
DR   STRING; 1075399.BLBCPU_345; -.
DR   KEGG; bcp:BLBCPU_345; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_10; -.
DR   Proteomes; UP000007112; Chromosome.
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; 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; GTPASE DER; 1.
DR   PANTHER; PTHR43834:SF6; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51712; G_ENGA; 1.
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..169
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         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         186..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         233..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         298..301
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   441 AA;  51353 MW;  DD5EE6BB5DC6F089 CRC64;
     MSYLVSIVGR PNVGKSTLFN RIIGKKKAIV HVKSGVTRDR IYGNSEWNGI QFSIVDTGGY
     NPPNNNIDII DTEIRKQILI ALKESDVILF LVDMEIGLLD VDIEISKILR KCKKSILLVV
     NKVDNGKNLY HDTDFFRLGF NNYYCISAIN GSGTGEMLDR LIEILKELVE KKVEEIGDIP
     RFSVIGRPNV GKSTLINSFL DKYRHIVTNI SGTTRDSIDV FYKKFGYKCI LFDTPGVRKK
     SKISENIEFY STMKTVRTIK YTDICFLMVD AVRGWESQDR NIFRLIEKNQ KGVIILINKW
     DLLHNNKNCS IKKNFEIFIK KNIAPFDNVP ILFISAKNKD GLYNIIPIAY HIFRKRKKRL
     KTNLLNRVMF PIFKKNPPPS INKKLITIKY CTQLPTYTPK FIFFSNYPQY IKESYKRFIE
     NKIRYHFDFI GVPIQIFFRK K
//
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