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Database: UniProt
Entry: K0DAL0_LEUCJ
LinkDB: K0DAL0_LEUCJ
Original site: K0DAL0_LEUCJ 
ID   K0DAL0_LEUCJ            Unreviewed;       437 AA.
AC   K0DAL0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   OrderedLocusNames=C270_04610 {ECO:0000313|EMBL:AFT81833.1};
OS   Leuconostoc carnosum (strain JB16).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT81833.1, ECO:0000313|Proteomes:UP000006299};
RN   [1] {ECO:0000313|EMBL:AFT81833.1, ECO:0000313|Proteomes:UP000006299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB16 {ECO:0000313|EMBL:AFT81833.1,
RC   ECO:0000313|Proteomes:UP000006299};
RX   PubMed=23144413; DOI=10.1128/JB.01805-12;
RA   Jung J.Y., Lee S.H., Jeon C.O.;
RT   "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT   from Kimchi.";
RL   J. Bacteriol. 194:6672-6673(2012).
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; CP003851; AFT81833.1; -; Genomic_DNA.
DR   RefSeq; WP_014974445.1; NC_018673.1.
DR   AlphaFoldDB; K0DAL0; -.
DR   STRING; 1229758.C270_04610; -.
DR   GeneID; 61186162; -.
DR   KEGG; lcn:C270_04610; -.
DR   PATRIC; fig|1229758.3.peg.923; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_9; -.
DR   Proteomes; UP000006299; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000006299};
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          176..352
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         182..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         230..234
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         295..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   437 AA;  48862 MW;  60CF7EE670BDA7F0 CRC64;
     MAAPIVAIVG RPNVGKSTIF NRMAGERIAI VEDQPGVTRD RLYAPAEWLN YEFRMIDTGG
     IELGDEPFLS EIRAQVELAI DEADVIVMVA SGREGLTSAD EVVAKMLYRT KKPVVLAINK
     VDNPEMRQDV YDFYALGLGD PFPVSGSHGL GLGDLLDEVV KHFPDEAAEQ EDDGVTRFSI
     IGRPNVGKSS IVNAMLGEER VIVSDIEGTT RDAIDTRFVT PEGDEFIMVD TAGMRKRGKV
     YENTEKYSVM RALKAIDNSS VILMVIDAEA GIREQDKHVA GFAHDAGRAM IIVVNKWDAI
     EKDDHTMKEF EEMIRVEFKF LDYAPVVFVS AKTGQRLERL PQLVKDVDSN HRKRISSSVL
     NDVIMDAIAV NPTPSDNGRR LRVYYATQVA TQPPTFVIFV NDVELMHFSY ERFLENKIRE
     AFDFTGTPVK LIVRARK
//
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