RBGA_BACSU
ID RBGA_BACSU Reviewed; 282 AA.
AC O31743;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribosome biogenesis GTPase A;
GN Name=rbgA; Synonyms=ylqF; OrderedLocusNames=BSU16050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION.
RX PubMed=16997968; DOI=10.1128/jb.01213-06;
RA Schaefer L., Uicker W.C., Wicker-Planquart C., Foucher A.-E., Jault J.-M.,
RA Britton R.A.;
RT "Multiple GTPases participate in the assembly of the large ribosomal
RT subunit in Bacillus subtilis.";
RL J. Bacteriol. 188:8252-8258(2006).
RN [3]
RP GTP- AND GDP-BINDING, PROTEIN LEVELS, AND DISRUPTION PHENOTYPE.
RC STRAIN=CRK6000;
RX PubMed=12427945; DOI=10.1099/00221287-148-11-3539;
RA Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
RA Ogasawara N.;
RT "Six GTP-binding proteins of the Era/Obg family are essential for cell
RT growth in Bacillus subtilis.";
RL Microbiology 148:3539-3552(2002).
RN [4]
RP FUNCTION, INTERACTION WITH CTC AND WITH THE 23S RIBOSOMAL RNA, AND SUBUNIT.
RX PubMed=16431913; DOI=10.1074/jbc.m512556200;
RA Matsuo Y., Morimoto T., Kuwano M., Loh P.C., Oshima T., Ogasawara N.;
RT "The GTP-binding protein YlqF participates in the late step of 50 S
RT ribosomal subunit assembly in Bacillus subtilis.";
RL J. Biol. Chem. 281:8110-8117(2006).
RN [5]
RP FUNCTION.
RX PubMed=16390447; DOI=10.1111/j.1365-2958.2005.04948.x;
RA Uicker W.C., Schaefer L., Britton R.A.;
RT "The essential GTPase RbgA (YlqF) is required for 50S ribosome assembly in
RT Bacillus subtilis.";
RL Mol. Microbiol. 59:528-540(2006).
RN [6]
RP FUNCTION.
RX PubMed=17613524; DOI=10.1074/jbc.m703894200;
RA Matsuo Y., Oshima T., Loh P.C., Morimoto T., Ogasawara N.;
RT "Isolation and characterization of a dominant negative mutant of Bacillus
RT subtilis GTP-binding protein, YlqF, essential for biogenesis and
RT maintenance of the 50 S ribosomal subunit.";
RL J. Biol. Chem. 282:25270-25277(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of the ylqF GTPase from B. subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
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. {ECO:0000269|PubMed:16390447,
CC ECO:0000269|PubMed:16431913, ECO:0000269|PubMed:16997968,
CC ECO:0000269|PubMed:17613524}.
CC -!- SUBUNIT: Interacts with ctc. Interacts with the immature 50S ribosome
CC subunit. 2 molecules of RbgA bind to one 50S subunit.
CC {ECO:0000269|PubMed:16431913, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. In
CC depletion experiments cells become over 3-fold longer, are abnormally
CC curved and nucleoids condense. {ECO:0000269|PubMed:12427945}.
CC -!- MISCELLANEOUS: Estimated to be present at 1000 copies per cell.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL009126; CAB13478.1; -; Genomic_DNA.
DR PIR; F69880; F69880.
DR RefSeq; NP_389487.1; NC_000964.3.
DR RefSeq; WP_009967235.1; NZ_JNCM01000035.1.
DR PDB; 1PUJ; X-ray; 2.00 A; A=1-282.
DR PDB; 6PPK; EM; 4.40 A; W=1-282.
DR PDBsum; 1PUJ; -.
DR PDBsum; 6PPK; -.
DR AlphaFoldDB; O31743; -.
DR SMR; O31743; -.
DR STRING; 224308.BSU16050; -.
DR PaxDb; O31743; -.
DR PRIDE; O31743; -.
DR EnsemblBacteria; CAB13478; CAB13478; BSU_16050.
DR GeneID; 940134; -.
DR KEGG; bsu:BSU16050; -.
DR PATRIC; fig|224308.179.peg.1745; -.
DR eggNOG; COG1161; Bacteria.
DR InParanoid; O31743; -.
DR OMA; GVLWPKF; -.
DR PhylomeDB; O31743; -.
DR BioCyc; BSUB:BSU16050-MON; -.
DR EvolutionaryTrace; O31743; -.
DR PRO; PR:O31743; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:CACAO.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..282
FT /note="Ribosome biogenesis GTPase A"
FT /id="PRO_0000360833"
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 BINDING 86..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 130..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1PUJ"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1PUJ"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1PUJ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1PUJ"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1PUJ"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:1PUJ"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:1PUJ"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:1PUJ"
SQ SEQUENCE 282 AA; 31986 MW; B69AD45877CF2573 CRC64;
MTIQWFPGHM AKARREVTEK LKLIDIVYEL VDARIPMSSR NPMIEDILKN KPRIMLLNKA
DKADAAVTQQ WKEHFENQGI RSLSINSVNG QGLNQIVPAS KEILQEKFDR MRAKGVKPRA
IRALIIGIPN VGKSTLINRL AKKNIAKTGD RPGITTSQQW VKVGKELELL DTPGILWPKF
EDELVGLRLA VTGAIKDSII NLQDVAVFGL RFLEEHYPER LKERYGLDEI PEDIAELFDA
IGEKRGCLMS GGLINYDKTT EVIIRDIRTE KFGRLSFEQP TM
