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Database: UniProt
Entry: A0A1Y4TKH9_9FIRM
LinkDB: A0A1Y4TKH9_9FIRM
Original site: A0A1Y4TKH9_9FIRM 
ID   A0A1Y4TKH9_9FIRM        Unreviewed;       443 AA.
AC   A0A1Y4TKH9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=B5E65_04955 {ECO:0000313|EMBL:OUQ43129.1};
OS   Gemmiger sp. An120.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX   NCBI_TaxID=1965549 {ECO:0000313|EMBL:OUQ43129.1, ECO:0000313|Proteomes:UP000195783};
RN   [1] {ECO:0000313|Proteomes:UP000195783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An120 {ECO:0000313|Proteomes:UP000195783};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUQ43129.1}.
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DR   EMBL; NFLN01000004; OUQ43129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TKH9; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000195783; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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:SF6; GTP-BINDING PROTEIN ENGA; 1.
DR   PANTHER; PTHR43834; 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   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
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:UP000195783};
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          4..169
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          178..353
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         184..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         231..235
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         296..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   443 AA;  49154 MW;  EB4EE2179EB404F1 CRC64;
     MPKPIVAVVG RPNVGKSTLF NKLIGQRLAI VEDTPGVTRD RIFGDCEWQN QKFLLVDTGG
     LEPNVDDGML LHMRQQAQLA IDSADCIIMV TDLRAGVTAL DQDVANLLMR SGKPVVLAVN
     KCDKVGEPPM ELYDFYSLGL GEVIPVSAVH GHGTGDLLDA VCAYLPKTEE NGEEDDRIPV
     AVIGRPNVGK SSLVNYILGE NRMIVANEAG TTRDAIDSPV ENQYGSFIFT DTAGLRKRSK
     VEDGVERYSV LRSLAAVERS RVCVILIDAT EGFTEQDSKV AGYAHEQGKA CIIAVNKWDA
     VEKDDKTMDA MRKKLMDDFS FMSYAPIIFI SARTGQRVDR LMELIRYVDG QNALRVTTGV
     LNELLARATA RVQPPSDKGK RLKIFYMTQA STRPPTFVCF INRAELFHFS YQRYIENQIR
     ETFGLEGTPV RLLVRERGDG KTR
//
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