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Database: UniProt
Entry: A0A348AQ63_9FIRM
LinkDB: A0A348AQ63_9FIRM
Original site: A0A348AQ63_9FIRM 
ID   A0A348AQ63_9FIRM        Unreviewed;       291 AA.
AC   A0A348AQ63;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Ribosome biogenesis GTPase A {ECO:0000256|ARBA:ARBA00014898, ECO:0000256|PIRNR:PIRNR006230};
GN   Name=rbgA {ECO:0000313|EMBL:BBB93211.1};
GN   ORFNames=MAMMFC1_03920 {ECO:0000313|EMBL:BBB93211.1};
OS   Methylomusa anaerophila.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Methylomusa.
OX   NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB93211.1, ECO:0000313|Proteomes:UP000276437};
RN   [1] {ECO:0000313|EMBL:BBB93211.1, ECO:0000313|Proteomes:UP000276437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMFC1 {ECO:0000313|EMBL:BBB93211.1,
RC   ECO:0000313|Proteomes:UP000276437};
RX   PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA   Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT   "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT   utilizing bacterium isolated from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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; AP018449; BBB93211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AQ63; -.
DR   KEGG; mana:MAMMFC1_03920; -.
DR   Proteomes; UP000276437; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; 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   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:UP000276437}.
FT   DOMAIN          13..178
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         130..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
FT   BINDING         174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
SQ   SEQUENCE   291 AA;  31929 MW;  393EA6663B633F59 CRC64;
     MHIHWFPGHM AKAQRMIREQ LKLIDVVIEL LDARIPYSSA NPVISEIIGE KPHVVALNKI
     DLAEPELTKQ WMSHFQNMNF SVVALDAASG NGMKNLIGQV EKIAGDKLAK LAAKGIKPRA
     VRAMILGIPN VGKSSLINRL LGSATVRTGD KPGVTRGQQW IKVGKNLELL DTPGVLWPKL
     DDQEIAFKLA ATGAIKDDVY DAEKVILKLV GLLRDDYSER LITRYNLPLP LPADDSELLG
     LIAARRGCLR SGGIVDYDKA GRIVLNEFRS GKLGGFTLDR PNTELDGMSN N
//
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