ID A0A3T0N6I9_9RHOB Unreviewed; 341 AA.
AC A0A3T0N6I9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:AZV79615.1};
GN ORFNames=EBB79_18230 {ECO:0000313|EMBL:AZV79615.1};
OS Parasedimentitalea marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV79615.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV79615.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV79615.1,
RC ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) 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; CP033219; AZV79615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0N6I9; -.
DR KEGG; sedi:EBB79_18230; -.
DR OrthoDB; 9809485at2; -.
DR Proteomes; UP000283063; 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; cd01854; YjeQ_EngC; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR InterPro; IPR010914; RsgA_GTPase_dom.
DR NCBIfam; TIGR00157; ribosome small subunit-dependent GTPase A; 1.
DR PANTHER; PTHR32120; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR PANTHER; PTHR32120:SF10; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR Pfam; PF03193; RsgA_GTPase; 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|HAMAP-Rule:MF_01820};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01820}; 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 91..245
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 97..243
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT REGION 307..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 188..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 273
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"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 341 AA; 37758 MW; 23472EC561F9D6D4 CRC64;
MTLTYSDLGW SNFFQSQQDA DADLTPYRIS AVHRDKLTGL SPDGEIQLLP DRLTGEFAVG
DWVLANAADQ VCERLERQTE LSRRAAGTDA REQLIAANVD VLFITTSCNA DFNLARLERY
LALAHQSGCY PVVVLTKADV CEDASVYRKQ AESLAASLTV LTLDAKNPDD VTQLLAWVKP
SQTATLVGSS GVGKTTLTNG LTGSKDAVRD IREDDSKGRH TTTARYLRRM VNGGWLIDTP
GMRALRIKDA DEGVEEVFSD LMEIAQGCRF NDCSHSGEPG CAVTAAVKEG TLELARVERW
QKLHRDEERN TETLVQSRRR DKGFGKMIKS MKRDHKGRKG Y
//
