ID A0A167T4K1_9BACI Unreviewed; 281 AA.
AC A0A167T4K1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000256|ARBA:ARBA00014898, ECO:0000256|PIRNR:PIRNR006230};
GN Name=ylqF {ECO:0000313|EMBL:ANB59440.1};
GN ORFNames=GFC30_1497 {ECO:0000313|EMBL:ANB59440.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB59440.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB59440.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB59440.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
CC -!- FUNCTION: Required for a late step of 50S ribosomal subunit assembly.
CC Has GTPase activity. {ECO:0000256|PIRNR:PIRNR006230}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006230}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000256|PIRNR:PIRNR006230}.
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DR EMBL; CP015438; ANB59440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167T4K1; -.
DR KEGG; aamy:GFC30_1497; -.
DR PATRIC; fig|294699.3.peg.1518; -.
DR OrthoDB; 9779790at2; -.
DR Proteomes; UP000076865; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd01856; YlqF; 1.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03596; GTPase_YlqF; 1.
DR PANTHER; PTHR45782; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 1; 1.
DR PANTHER; PTHR45782:SF4; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF006230; MG442; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006230};
KW GTP-binding {ECO:0000256|PIRNR:PIRNR006230, ECO:0000256|PIRSR:PIRSR006230-
KW 1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006230,
KW ECO:0000256|PIRSR:PIRSR006230-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 14..179
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT BINDING 58..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
FT BINDING 131..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
FT BINDING 175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
SQ SEQUENCE 281 AA; 31141 MW; 7FE9F667E088792F CRC64;
MTIQWFPGHM AKAKREVQEK LKLIDVVFEL LDARIPLSSR NPMIDEILTN KPRIILLNKA
DMADEKVTSE WISFFAEQGM PAIAIDAQAG TGMKQIVAAA KEMTKEKFAK MAAKGIKNPR
PMRALIVGIP NVGKSTLINR LAGKHIAKTG DKPGVTKAQQ WIKVGKEMEL LDTPGILWPK
FEDEEVGLKL ATTGAIKDTI LNLQDVAVYA LRFLAAHYPD RLKERYSLAA IPDDIVELFD
AIGKRRGCLA SGGAVDYDKV AELVLRDIRT EKLGRLSLEK P
//
