ID   A0A7W3LIQ5_ACTNM        Unreviewed;       330 AA.
AC   A0A7W3LIQ5;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   29-SEP-2021, entry version 2.
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=HNR61_000505 {ECO:0000313|EMBL:MBA8948907.1};
OS   Actinomadura namibiensis.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Actinomadura.
OX   NCBI_TaxID=182080 {ECO:0000313|EMBL:MBA8948907.1, ECO:0000313|Proteomes:UP000572680};
RN   [1] {ECO:0000313|EMBL:MBA8948907.1, ECO:0000313|Proteomes:UP000572680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44197 {ECO:0000313|EMBL:MBA8948907.1,
RC   ECO:0000313|Proteomes:UP000572680};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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:MBA8948907.1}.
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DR   EMBL; JACJIA010000001; MBA8948907.1; -; Genomic_DNA.
DR   Proteomes; UP000572680; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00157; TIGR00157; 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|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01820};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000313|EMBL:MBA8948907.1};
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}.
FT   DOMAIN          109..263
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          118..261
FT                   /note="ENGC_GTPASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   NP_BIND         158..161
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   NP_BIND         204..212
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  35801 MW;  0A7D39C3B51D4561 CRC64;
     MARRARDYDE DDVRVRPSRR GSRPRTRIRP AHEDAVEGFV VAVDRGRYRC LVEDRTVTAM
     RARELGRKGV VVGDRVALVG DVSGRPDTLA RIVRVEPRGS TLRRTADDTD PFERIIVANA
     DQLAIVTALA DPEPRPRLID RQLVAAYDAG MHPLLVLTKA DLADPDALLA EYASLGVPAF
     VTQRGGDLAG LRDLLRGQIT VLVGHSGVGK STLVNALVPD AERAVSHVNA VTGRGRHTSS
     SALALELPDG EGWIIDTPGV RSFGLAHVRP ENVINAFEDL AEGAAERCPP HCDHLQSECG
     LDSWVADGHA SQGRLDSLRR LLRSREGEAD
//