RBGA_BACLD
ID RBGA_BACLD Reviewed; 283 AA.
AC Q65JP4; Q62V49;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000250|UniProtKB:O31743};
GN Name=rbgA {ECO:0000312|EMBL:AAU23360.1};
GN Synonyms=ylqF {ECO:0000312|EMBL:AAU40720.1};
GN OrderedLocusNames=BL01289, BLi01825;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1] {ECO:0000312|EMBL:AAU23360.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46 {ECO:0000312|EMBL:AAU23360.1};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [2] {ECO:0000312|EMBL:AAU40720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46 {ECO:0000312|EMBL:AAU40720.1};
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
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; CP000002; AAU23360.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU40720.1; -; Genomic_DNA.
DR RefSeq; WP_003181730.1; NC_006322.1.
DR AlphaFoldDB; Q65JP4; -.
DR SMR; Q65JP4; -.
DR STRING; 279010.BL01289; -.
DR EnsemblBacteria; AAU23360; AAU23360; BL01289.
DR GeneID; 66216164; -.
DR KEGG; bld:BLi01825; -.
DR KEGG; bli:BL01289; -.
DR eggNOG; COG1161; Bacteria.
DR HOGENOM; CLU_011106_1_0_9; -.
DR OMA; GVLWPKF; -.
DR OrthoDB; 1083771at2; -.
DR BioCyc; BLIC279010:BLI_RS09020-MON; -.
DR Proteomes; UP000000606; 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; Reference proteome;
KW Ribosome biogenesis; RNA-binding.
FT CHAIN 1..283
FT /note="Ribosome biogenesis GTPase A"
FT /id="PRO_0000409881"
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 283 AA; 31945 MW; B93133688DB2BE55 CRC64;
MVIQWFPGHM AKARREVTEK LKLIDIVYEL VDARIPMSSR NPMIEDILKN KPRIMLLNKA
DKADSSVTKA WKQHFEKDGI PTLAINSVNG QGLNQILPAS KELLKEKFDK MKAKGVKPRA
IRALIVGIPN VGKSTLINRL AKKNIAKTGD RPGVTTAQQW VKVGKELELL DTPGILWPKF
EDELVGLRLA ATGAIKDSII NLQDVAVYGL RFLEENYPER LKKRYDLEEI PEEIAALFDE
IGKKRGCLMA GGEINYDKTT EVIIRDIRTE KFGPLSFEKP EDM
