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Database: UniProt
Entry: K4KH52_SIMAS
LinkDB: K4KH52_SIMAS
Original site: K4KH52_SIMAS 
ID   K4KH52_SIMAS            Unreviewed;       312 AA.
AC   K4KH52;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Ribosome biogenesis GTPase A {ECO:0000256|PIRNR:PIRNR006230};
GN   Name=rbgA {ECO:0000313|EMBL:AFU97268.1};
GN   OrderedLocusNames=M5M_00155 {ECO:0000313|EMBL:AFU97268.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU97268.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFU97268.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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; CP003746; AFU97268.1; -; Genomic_DNA.
DR   RefSeq; WP_015045441.1; NZ_ATUQ01000015.1.
DR   AlphaFoldDB; K4KH52; -.
DR   STRING; 1117647.M5M_00155; -.
DR   KEGG; saga:M5M_00155; -.
DR   eggNOG; COG1161; Bacteria.
DR   HOGENOM; CLU_011106_1_0_6; -.
DR   OrthoDB; 9779790at2; -.
DR   Proteomes; UP000000466; 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; 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.
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:UP000000466}.
FT   DOMAIN          118..188
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
FT   BINDING         125..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
FT   BINDING         169
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
SQ   SEQUENCE   312 AA;  34671 MW;  5A1F1058C11AEB1D CRC64;
     MSIQWYPGHM HKARKQMLEL LPRIDVLVEI LDARVPHSSQ NPVIAEACTH LPVIKLLSKD
     DLADPAMTQA WQTHFEQQDN TRTLAVDLRM PGKLKSLIPE LVRKLAPTKA EQNRTINVLV
     AGIPNVGKST FINTMAGRPA AKTGNEPAVT KAQQQINLED GVILFDSPGM LWPKLEHNNT
     GFRLAATSAI KNTVIDFEDL GLYLADYLLP NYPEGLKERY GLKSLPKDSL GLISAVCQRR
     GGMKANEVDY YKGGEILVSD FRAARLGRIT LETPEVIAQE LLEVEQARAL KAERDAEKEA
     KKALKKAGKR HT
//
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