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Database: UniProt
Entry: G8UK87_TANFA
LinkDB: G8UK87_TANFA
Original site: G8UK87_TANFA 
ID   G8UK87_TANFA            Unreviewed;       310 AA.
AC   G8UK87;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820,
GN   ECO:0000313|EMBL:AEW20370.1};
GN   OrderedLocusNames=BFO_1340 {ECO:0000313|EMBL:AEW20370.1};
OS   Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS   5666 / FDC 338) (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW20370.1, ECO:0000313|Proteomes:UP000005436};
RN   [1] {ECO:0000313|Proteomes:UP000005436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC   {ECO:0000313|Proteomes:UP000005436};
RA   Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA   Shetty J., Torralba M., Gill S., Nelson K.;
RT   "Complete sequence of Tannerella forsythia ATCC 43037.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of several proteins that assist in the late maturation
CC       steps of the functional core of the 30S ribosomal subunit. Helps
CC       release RbfA from mature subunits. May play a role in the assembly of
CC       ribosomal proteins into the subunit. Circularly permuted GTPase that
CC       catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S
CC       ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01820};
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01820}.
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DR   EMBL; CP003191; AEW20370.1; -; Genomic_DNA.
DR   RefSeq; WP_014224708.1; NC_016610.1.
DR   AlphaFoldDB; G8UK87; -.
DR   STRING; 203275.BFO_1340; -.
DR   GeneID; 34758544; -.
DR   KEGG; tfo:BFO_1340; -.
DR   PATRIC; fig|203275.8.peg.1205; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_0_10; -.
DR   OMA; CLVAAYD; -.
DR   Proteomes; UP000005436; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd04466; S1_YloQ_GTPase; 1.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   InterPro; IPR031944; RsgA_N.
DR   NCBIfam; TIGR00157; ribosome small subunit-dependent GTPase A; 1.
DR   PANTHER; PTHR32120; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR   PANTHER; PTHR32120:SF11; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   Pfam; PF16745; RsgA_N; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01820};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01820};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01820};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01820}; Reference proteome {ECO:0000313|Proteomes:UP000005436};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   DOMAIN          77..238
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          86..236
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         180..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   310 AA;  34492 MW;  D82D071C43331242 CRC64;
     MHGLVVKNTG SRYTVHTDDG RSVDCKIKGS FRLKGIRSTN PVTIGDRVEI EENREGSACI
     TAIDARRNYM IRRASNLSKE SHILAANIDL ALLVVTIHYP QTTTTFIDRF LATAEAYGIP
     ALLVFNKTDR YDADELEYVE ELMTLYRTIG YDCMKLCAAS GEGIDALSDK ISNRITLLSG
     HSGVGKSTII NKLLPHAKLR TKDISEYHQT GVHTTTFSEM IPLPNGGYLI DTPGIKGFGT
     IEMQGGEVAH YFPEIFKHSA DCRFSNCTHT HEPGCAVREA VEAHSISRSR YKSYLNILED
     MDGAKYREAY
//
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