RSGA_DICD3
ID RSGA_DICD3 Reviewed; 349 AA.
AC Q9EV05; E0SI23;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820};
GN OrderedLocusNames=Dda3937_02151;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-349.
RC STRAIN=3937;
RX PubMed=11679069; DOI=10.1046/j.1365-2958.2001.02591.x;
RA Touze T., Gouesbet G., Boiangiu C., Jebbar M., Bonnassie S., Blanco C.;
RT "Glycine betaine loses its osmoprotective activity in a bspA strain of
RT Erwinia chrysanthemi.";
RL Mol. Microbiol. 42:87-99(2001).
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:0000255|HAMAP-Rule:MF_01820}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820};
CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
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DR EMBL; CP002038; ADN00232.1; -; Genomic_DNA.
DR EMBL; AJ251781; CAC18670.1; -; Genomic_DNA.
DR RefSeq; WP_013319650.1; NC_014500.1.
DR AlphaFoldDB; Q9EV05; -.
DR SMR; Q9EV05; -.
DR STRING; 198628.Dda3937_02151; -.
DR EnsemblBacteria; ADN00232; ADN00232; Dda3937_02151.
DR GeneID; 9735514; -.
DR KEGG; ddd:Dda3937_02151; -.
DR PATRIC; fig|198628.6.peg.3972; -.
DR eggNOG; COG1162; Bacteria.
DR HOGENOM; CLU_033617_2_0_6; -.
DR OMA; CLVAAYD; -.
DR OrthoDB; 908180at2; -.
DR BioCyc; DDAD198628:DDA3937_RS18945-MON; -.
DR Proteomes; UP000006859; 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; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..349
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000171476"
FT DOMAIN 111..272
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 212..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT CONFLICT 82..83
FT /note="RA -> AP (in Ref. 2; CAC18670)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..97
FT /note="ISGIVEA -> HQRHRRKR (in Ref. 2; CAC18670)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="L -> F (in Ref. 2; CAC18670)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..299
FT /note="Missing (in Ref. 2; CAC18670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38943 MW; 9F1A44F6ED4578B3 CRC64;
MSKKKLSKGQ QRRVSANHQR RLKHADSKVE WDDSQLSEPQ EGVIISRFGM HADVEAPDGK
LHRCNIRRTI HSLVTGDRVV WRAGNETLAG ISGIVEAVHP RQSVLTRPDY YDGLKPIAAN
IDQIVIVSAI LPELSLNIID RYLVACETLE IEPLIVLNKI DLLDDEGRAF VEEVMDIYRA
LHYRVLMMSS HTQQGVAELE AALTGRVSIF AGQSGVGKSS LLNALLYPDD AQILVNDVSD
ASGLGQHTTT AARLYHFPHG GDVIDSPGVR EFGLWHLEPE QVTRGFIEFR DYLGSCKFRD
CKHDTDPGCA IRAALERGEI APERFDNYHR ILESMAQVKT RKSFSAPDN
