RSGA_PSEAE
ID RSGA_PSEAE Reviewed; 339 AA.
AC Q9HUL3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=PA4952;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08337.1; -; Genomic_DNA.
DR PIR; F83026; F83026.
DR RefSeq; NP_253639.1; NC_002516.2.
DR RefSeq; WP_003113927.1; NZ_QZGE01000002.1.
DR PDB; 6H4D; X-ray; 2.90 A; A=1-339.
DR PDBsum; 6H4D; -.
DR AlphaFoldDB; Q9HUL3; -.
DR SMR; Q9HUL3; -.
DR STRING; 287.DR97_2305; -.
DR PaxDb; Q9HUL3; -.
DR PRIDE; Q9HUL3; -.
DR EnsemblBacteria; AAG08337; AAG08337; PA4952.
DR GeneID; 878216; -.
DR KEGG; pae:PA4952; -.
DR PATRIC; fig|208964.12.peg.5185; -.
DR PseudoCAP; PA4952; -.
DR HOGENOM; CLU_033617_2_0_6; -.
DR InParanoid; Q9HUL3; -.
DR OMA; CLVAAYD; -.
DR PhylomeDB; Q9HUL3; -.
DR BioCyc; PAER208964:G1FZ6-5068-MON; -.
DR Proteomes; UP000002438; 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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00157; TIGR00157; 1.
DR PROSITE; PS50936; ENGC_GTPASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding; Zinc.
FT CHAIN 1..339
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000171505"
FT DOMAIN 111..271
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 213..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:6H4D"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6H4D"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6H4D"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:6H4D"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:6H4D"
SQ SEQUENCE 339 AA; 37078 MW; FCC83A1CC2DF517B CRC64;
MAKRHLTRRQ SWRIEKIQEE RAARAARRES RAVEELEGGD LGPEQTGQVI AHFGVQVEVE
SADGQVSRCH LRANLPALVT GDQVVWRAGN QGIGVIVAQL PRRSELCRPD MRGLLKPVAA
NVDRIVIVFA PRPEPHANLI DRYLIAAEHA GIQPLLLLNK ADLVDESNAE GIDALLNVYR
TLGYPLIEVS AFNGLAMDEL RGALDGHVSV FVGQSGVGKS SLVNALLPGV DTRVGDLSTV
TGKGTHTTTT ARLFHFPGGG DLIDSPGIRE FGLGHVSRDD VEAGFIEFRD LLGHCRFRDC
KHDREPGCAL LQALEDGRIM PQRMASYRHI LASMPETDY
