ID F9MQG9_9FIRM Unreviewed; 294 AA.
AC F9MQG9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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:EGS32442.1};
GN ORFNames=HMPREF1040_1232 {ECO:0000313|EMBL:EGS32442.1};
OS Megasphaera sp. UPII 135-E.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS32442.1, ECO:0000313|Proteomes:UP000004137};
RN [1] {ECO:0000313|EMBL:EGS32442.1, ECO:0000313|Proteomes:UP000004137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS32442.1,
RC ECO:0000313|Proteomes:UP000004137};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGS32442.1}.
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DR EMBL; AFUG01000040; EGS32442.1; -; Genomic_DNA.
DR AlphaFoldDB; F9MQG9; -.
DR eggNOG; COG1162; Bacteria.
DR OrthoDB; 9809485at2; -.
DR Proteomes; UP000004137; Unassembled WGS sequence.
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:UP000004137};
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 68..224
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 77..222
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT BINDING 167..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 294 AA; 33110 MW; 67EB1433A3F28BEF CRC64;
MYECSSEKQT GRVIKNYNGY YYVDLSEPTL RECRRRGKVK HKILVGDEVE VMATDHGKGL
IEAVLPRQNE LRRPAVANID QIVMVLAAQS PDPDYFLTDK LLLTCAYHHI SPLLCMNKSE
LQREVAQAYC QHYTQCGYKT LAVSAHTGEG IDLLRSYLQG KITAFSGPSG VGKSSLLTLL
LGKELATGAV SEKIRRGRHT TRHAEMLCMD AHTYVVDTPG FAAIELEPLK VAKLALLFPE
FKPYVGQCRF PSCVHVHEPD CAIKEAKERG EISETRYMTY CKLLHEIKER KSFV
//