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Database: UniProt
Entry: A0A0D6DZD6_9LACT
LinkDB: A0A0D6DZD6_9LACT
Original site: A0A0D6DZD6_9LACT 
ID   A0A0D6DZD6_9LACT        Unreviewed;       436 AA.
AC   A0A0D6DZD6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=LACPI_1639 {ECO:0000313|EMBL:CEN28839.1};
OS   Lactococcus piscium MKFS47.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN28839.1, ECO:0000313|Proteomes:UP000033166};
RN   [1] {ECO:0000313|Proteomes:UP000033166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA   Andreevskaya M.;
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; LN774769; CEN28839.1; -; Genomic_DNA.
DR   RefSeq; WP_047915897.1; NZ_LN774769.1.
DR   AlphaFoldDB; A0A0D6DZD6; -.
DR   STRING; 1364.LP2241_50031; -.
DR   KEGG; lpk:LACPI_1639; -.
DR   HOGENOM; CLU_016077_6_2_9; -.
DR   Proteomes; UP000033166; Chromosome I.
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   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          4..167
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          175..351
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         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         181..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   436 AA;  48880 MW;  0A83F0AACF89A979 CRC64;
     MALPTVAIVG RPNVGKSTIF NRIAGERISI VEDIPGITRD RIYTTSEWLN NKFAMIDTGG
     IEMADTPFMS QIKAQAEIAM DEADVIVFVV DGENGVTDAD EYVAQILYKT DTPVILVVNK
     IDNPERRMEI FDFYSLGLGE PYPVSAVHGI GTGDVLDAIV ENLPVDTEEE NPDIIKFSLI
     GRPNVGKSSL INAILGEDRV IASPIAGTTR DAIDTNFTDA EGQEFTMIDT AGMRKRGKVY
     ESTEKYSVMR AMRAIDRSDV VLMILNAEEG IREYDKRIAG FAHEAGRGII IVVNKWDTIE
     KDNKTLKNWE EKIRDEFQYL SYAPIIFVSA ETKQRLHKLP ELIKAVSQAQ NMRIPSAVLN
     DVIMDAIAIN PTPTDKGRRL KIFYATQVAI KPPTFVVFVN EEELMHFSYG RMLENQIRKA
     FVFEGTPIHL ISRKRK
//
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