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Database: UniProt
Entry: A0A139STA5_9BACT
LinkDB: A0A139STA5_9BACT
Original site: A0A139STA5_9BACT 
ID   A0A139STA5_9BACT        Unreviewed;       532 AA.
AC   A0A139STA5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=AXK12_01190 {ECO:0000313|EMBL:KXU37807.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU37807.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU37807.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU37807.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU37807.1}.
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DR   EMBL; LSZP01000004; KXU37807.1; -; Genomic_DNA.
DR   RefSeq; WP_068710833.1; NZ_LSZP01000004.1.
DR   AlphaFoldDB; A0A139STA5; -.
DR   STRING; 1548208.AXK12_01190; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000071392; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000071392};
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          205..398
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   REGION          172..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         61..65
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         127..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         211..218
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         263..267
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         328..331
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   532 AA;  58913 MW;  658B5D7E1119AA10 CRC64;
     MSSHARTQNR IVAIVGRPNV GKSRLFNRLA RRRISIVHDE AGITRDVIST EIEEGRYTLL
     DTSGLGLTGS DTPQRITAAA EQQVDFAIDT AGLILFVIDG LSGTTALDEQ IARKLRRAKA
     KVRLVVNKAD FDEARVDLAE AYRFGLGEPI SVSAEHGHGE GRLREAILDA LGPAPEPDGE
     ADDAGVENAE EAAPQPYKSR EKRPLRLCFL GRPNVGKSSL SNRLLASERL IVSDMPGTTR
     DAVELPFTFT GRNGRSYPFS LIDTAGIKAA TKLAAPVEYF SRLRSLDAIQ RADVVFLVLD
     ALEGVTQQDK AIAGEAVKER KPIVVVVNKW DLVHAAFEKP EGLKGFASER DYREKYERAV
     FERLFFTPGA PLIFASAHSE LALDRMMNAA VKLDRTLEKK LPTGRLNRLL AELTERTPPP
     VVGSRRFRIY YATQTGRRPF RIRIFCNRED RLPESYRRYL ESGVIREFKL EGCPVYFDLV
     GKEKHTPGAS YTSRKNSAGT EAHSPTPAKW RSAEAAELGA DNFGGDYTTL ED
//
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