RBGA_BACSH
ID RBGA_BACSH Reviewed; 282 AA.
AC E0TTS5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000250|UniProtKB:O31743, ECO:0000312|EMBL:ADM37701.1};
GN Name=rbgA; Synonyms=ylqF {ECO:0000250|UniProtKB:O31743};
GN OrderedLocusNames=BSUW23_08265;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(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; CP002183; ADM37701.1; -; Genomic_DNA.
DR RefSeq; WP_003220827.1; NC_014479.1.
DR AlphaFoldDB; E0TTS5; -.
DR SMR; E0TTS5; -.
DR EnsemblBacteria; ADM37701; ADM37701; BSUW23_08265.
DR GeneID; 64303497; -.
DR KEGG; bss:BSUW23_08265; -.
DR HOGENOM; CLU_011106_1_0_9; -.
DR OMA; GVLWPKF; -.
DR Proteomes; UP000002233; 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 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..282
FT /note="Ribosome biogenesis GTPase A"
FT /id="PRO_0000409882"
FT DOMAIN 14..178
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 86..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 130..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
SQ SEQUENCE 282 AA; 32000 MW; B09CD45E71CF2573 CRC64;
MTIQWFPGHM AKARREVTEK LKLIDIVYEL VDARIPMSSR NPMIEDILKN KPRIMLLNKA
DKADAAVTQQ WKEHFENQGI RSLSINSVNG QGLNQIVPAS KEILQEKFDR MRAKGVKPRA
IRALIIGIPN VGKSTLINRL AKKNIAKTGD RPGITTSQQW VKVGKELELL DTPGILWPKF
EDELVGLRLA VTGAIKDSII NLQDVAVFGL RFLEEHYPER LKERYALDEI PEDIAELFDA
IGEKRGCLMS GGLINYDKTT EVIIRDIRTE KFGRLSFEQP TM