RBGA_PRIM3
ID RBGA_PRIM3 Reviewed; 288 AA.
AC D5DJL5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000312|EMBL:ADF41024.1};
GN Name=rbgA {ECO:0000312|EMBL:ADF41024.1};
GN Synonyms=ylqF {ECO:0000250|UniProtKB:O31743}; OrderedLocusNames=BMD_4194;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1] {ECO:0000312|EMBL:ADF41024.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521 {ECO:0000312|EMBL:ADF41024.1};
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
CC -!- FUNCTION: Essential protein that is required for a late step of 50S
CC ribosomal subunit assembly. Has GTPase activity that is stimulated by
CC interaction with the immature 50S ribosome subunit. Binds to the 23S
CC rRNA. Required for the association of ribosomal proteins rplP and rpmA
CC with the large subunit (By similarity). {ECO:0000250|UniProtKB:O31743}.
CC -!- SUBUNIT: Interacts with ctc. Interacts with the immature 50S ribosome
CC subunit. 2 molecules of rbgA bind to one 50S subunit (By similarity).
CC {ECO:0000250|UniProtKB:O31743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O31743,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; CP001982; ADF41024.1; -; Genomic_DNA.
DR RefSeq; WP_013084807.1; NC_014103.1.
DR AlphaFoldDB; D5DJL5; -.
DR SMR; D5DJL5; -.
DR EnsemblBacteria; ADF41024; ADF41024; BMD_4194.
DR KEGG; bmd:BMD_4194; -.
DR PATRIC; fig|592022.4.peg.4191; -.
DR HOGENOM; CLU_011106_1_0_9; -.
DR OMA; GVLWPKF; -.
DR Proteomes; UP000002365; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR019991; GTP-bd_ribosome_bgen.
DR InterPro; IPR016478; GTPase_MTG1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF006230; MG442; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03596; GTPase_YlqF; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Ribosome biogenesis;
KW RNA-binding.
FT CHAIN 1..288
FT /note="Ribosome biogenesis GTPase A"
FT /id="PRO_0000409884"
FT DOMAIN 14..179
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 58..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 131..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
SQ SEQUENCE 288 AA; 32618 MW; D31091C1AA5CFCB1 CRC64;
MTIQWFPGHM AKARRQVTEK LKLIDIVYEL VDARIPQSSR NPMIDEIIVN KPRIVLLNKV
DKADPRVTQQ WLDYYKEQGI YALAIDAQAG KGMKQIVSSS KELLQEKFDR MRAKGVKKPR
AIRAMIVGIP NVGKSTLINR LASKKIAKTG DRPGVTQAQQ WIKVGNELEL LDTPGILWPK
FEDETVGYKL ATTGAIKDTI LNMQDVAVYA LRFLTSHYPE QLKQRYNLNE IPEDIVELFD
AIGSRRGCLM GGGMVDYDKT AELVLREIRT DKIGTFTFDD PSEAEQPL