ID A0A0F4QQR0_9GAMM Unreviewed; 490 AA.
AC A0A0F4QQR0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=TW77_11205 {ECO:0000313|EMBL:KJZ08942.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ08942.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ08942.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ08942.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ08942.1}.
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DR EMBL; JXYA01000023; KJZ08942.1; -; Genomic_DNA.
DR RefSeq; WP_046005068.1; NZ_JXYA01000023.1.
DR AlphaFoldDB; A0A0F4QQR0; -.
DR PATRIC; fig|43658.5.peg.2368; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000033452; 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; 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 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:UP000033452};
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..166
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 203..376
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 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 209..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 256..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 321..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 490 AA; 54645 MW; 07E8C6ABAF91940B CRC64;
MLPVIALVGR PNVGKSTLFN RLTRTRDALV ADFPGLTRDR KYGQANYDGY EFIVVDTGGI
DGSEEGIETE MAEQSLLAIE EADVVLFLVD ARAGMTAADQ AIAQHLRKQQ KKSFVVANKT
DGIDADSNCA EFYQLALGEV YHIAAAHGRG VTQLLEATLG PVIAELAGEE DDIEQDDELL
TELYLEGEEA PDDGKTGFED KPIKLAIIGR PNVGKSTLTN RILGEERVIV YDMPGTTRDS
IYIPMTRNER DYVLIDTAGV RKRKKVSDVV EKFSVIKTLQ AIEDANVILL VIDARDGISD
QDLSLLGFAL NAGRSLVIAV NKWDGLDDYV KERIKSELDR RLGFIDFARL HFISALHGTG
VGHLFESVEE AYESATKRVS TAMLRRIMDM AQADHQPPLV RGRRVKLKYA HAGGYNPPRI
VIHGNQVHDL PDSYKRYLMN YYRKALNIMG TPIKIEFREG DNPYAGRTNK MTLSQKRKLR
AFTKEQKNKS
//
