ID A0A095WN12_9ACTO Unreviewed; 356 AA.
AC A0A095WN12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HMPREF1627_08735 {ECO:0000313|EMBL:KGE99234.1};
OS Actinomyces sp. S6-Spd3.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1284680 {ECO:0000313|EMBL:KGE99234.1, ECO:0000313|Proteomes:UP000029604};
RN [1] {ECO:0000313|EMBL:KGE99234.1, ECO:0000313|Proteomes:UP000029604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-Spd3 {ECO:0000313|EMBL:KGE99234.1,
RC ECO:0000313|Proteomes:UP000029604};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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 -!- 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:KGE99234.1}.
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DR EMBL; JRMV01000281; KGE99234.1; -; Genomic_DNA.
DR RefSeq; WP_034502854.1; NZ_JRMV01000281.1.
DR AlphaFoldDB; A0A095WN12; -.
DR PATRIC; fig|1284680.3.peg.1456; -.
DR eggNOG; COG1162; Bacteria.
DR Proteomes; UP000029604; 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: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:SF11; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA 1, MITOCHONDRIAL-RELATED; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01820}; Reference proteome {ECO:0000313|Proteomes:UP000029604};
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}.
FT DOMAIN 110..266
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 119..264
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 208..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 356 AA; 38445 MW; 1955279C6341A123 CRC64;
MSRRDIGTDD PRVKVRPSKR SRPRTKVRPD WGNKPIGQVI GIDRGRYLVR YEGLDLRAVL
ARELKKGSVV VGDRVRLTGD LSGRVDTLAR IVATDERSSV LRRSLEDAPD QKGEKIIVAN
AQIMVIVTAL ADPPPRMGMI DRCLVAAHEA GMRAVLCLTK ADLAPATEFL EAYADFDVTT
VVTSVEAGCQ GLDELKEILA GHFSVLVGHS GVGKSTLINA LIPQAERVVG VVNQVTGRGR
HTSTSSRAFE LPGGGWIVDT PGVRSFGLGH VDIDDVLGVF PDVAEASRWC LPLCTHLEDA
TSCALDAWAQ GKDPFVISST DEAADQERRR RSSRVASVRR LLDAVAGAMK VSKAAR
//
