ID A0A1Y2KB83_9PROT Unreviewed; 341 AA.
AC A0A1Y2KB83;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=MAIT1_00008 {ECO:0000313|EMBL:OSM07075.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM07075.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM07075.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM07075.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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: 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:OSM07075.1}.
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DR EMBL; LVJN01000015; OSM07075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2KB83; -.
DR STRING; 1434232.MAIT1_00008; -.
DR Proteomes; UP000194003; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000194003};
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 90..247
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 98..245
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 189..197
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 270
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 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 341 AA; 37210 MW; 3E079009DF4374FF CRC64;
MGFGPFFQQQ LSLDEFDAAT PARVTARDGL ILQLITPSGF QRLTLPGGWR ALPVDEQPVV
GDWLLLDAAG VAQRLLERSS FLARRAAGHG HHLQPMAANL STLFIVTSCN QDFNPSRLER
YLTLAQEGGA APVIVLTKAD LLENPADLLR QAQRLAPGLI ALALDARQTE ARTLLAPWLG
EGETVAFVGS SGVGKSTLIN TLRGEAAQAT GAIREDDAHG RHTTTSRQLL PLEGGAWLLD
TPGMRELRVE ASDAGLEAVF ADVAALAERC RFRDCGHQQD DGCAVRAAVD DGEIDVRRLE
NFLKLQREQG YLRESAHESR DRQRKFSKMV NSAKVTKFGR R
//
