ID A0A2A3XIS7_9GAMM Unreviewed; 467 AA.
AC A0A2A3XIS7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:PCC23596.1};
GN ORFNames=CIK78_16925 {ECO:0000313|EMBL:PCC23596.1};
OS Halomonas sp. JB37.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2024405 {ECO:0000313|EMBL:PCC23596.1, ECO:0000313|Proteomes:UP000217454};
RN [1] {ECO:0000313|EMBL:PCC23596.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB37 {ECO:0000313|EMBL:PCC23596.1};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
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:PCC23596.1}.
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DR EMBL; NRGW01000001; PCC23596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3XIS7; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000217454; 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; 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};
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 178..351
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT REGION 432..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
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: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 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 467 AA; 51602 MW; 183EDB0CEE646E9C CRC64;
MTPVIALVGR PNVGKSTLFN RLTRSRDALV ADFPGLTRDR KYGNGMLGDK VYTVIDTGGI
SGDEEGIDAA MAEQSLAAID EADIVLFMVD ARAGLMPADQ AIANHLRVNQ KKTWLVVNKT
DGLEEHSAMG DFWSLGLGDP WPIAAAHGRN VSTLIDVVLE PFPERDASIP ADTGSKGVRI
GVIGRPNVGK STLVNRLLGE DRVVVFDEAG TTRDSIEIPF ERRGKPYVLI DTAGIRRRKN
VREITEKFSI IKTLDAIKES HVVIMVLDGS SGLVEQDLHL LDYVLTTGRA LVLAVNKWDG
LESEAKEKMR VEIKRRLGFA DYAELHFISA LHGTAVGDLY PSIDRAFDAA NAHWSTNRLT
TLLQDAVSQN PPPMVQGRRI KLRMAHQGGS NPPIIVVHGN QTESVPEAYR RYLTNTFRKV
LKVRGTPIRF EFRSGSNPFD HMAGASDKEK AKKRELNRTK EARKSRR
//
