RSGA_STAAC
ID RSGA_STAAC Reviewed; 291 AA.
AC Q9KX08;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SACOL1234;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10566865; DOI=10.1089/mdr.1999.5.163;
RA de Lencastre H., Wu S.-W., Pinho M.G., Ludovice A.M., Filipe S.,
RA Gardete S., Sobral R., Gill S.R., Chung M., Tomasz A.;
RT "Antibiotic resistance as a stress response: complete sequencing of a large
RT number of chromosomal loci in Staphylococcus aureus strain COL that impact
RT on the expression of resistance to methicillin.";
RL Microb. Drug Resist. 5:163-175(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; Y13639; CAA73981.1; -; Genomic_DNA.
DR EMBL; CP000046; AAW38069.1; -; Genomic_DNA.
DR RefSeq; WP_000847933.1; NC_002951.2.
DR PDB; 6ZJO; X-ray; 2.01 A; A/B=1-291.
DR PDBsum; 6ZJO; -.
DR AlphaFoldDB; Q9KX08; -.
DR SMR; Q9KX08; -.
DR EnsemblBacteria; AAW38069; AAW38069; SACOL1234.
DR KEGG; sac:SACOL1234; -.
DR HOGENOM; CLU_033617_2_1_9; -.
DR OMA; CLVAAYD; -.
DR Proteomes; UP000000530; 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; cd04466; S1_YloQ_GTPase; 1.
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 InterPro; IPR031944; RsgA_N.
DR PANTHER; PTHR32120; PTHR32120; 1.
DR Pfam; PF03193; RsgA_GTPase; 1.
DR Pfam; PF16745; RsgA_N; 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; Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..291
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000171513"
FT DOMAIN 63..221
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 112..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 164..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:6ZJO"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6ZJO"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:6ZJO"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:6ZJO"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6ZJO"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:6ZJO"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:6ZJO"
SQ SEQUENCE 291 AA; 33890 MW; 3D7FE2B5989577D6 CRC64;
MKTGRIVKSI SGVYQVDVNG ERFNTKPRGL FRKKKFSPVV GDIVEFEVQN INEGYIHQVF
ERENELKRPP VSNIDTLVIV MSAVEPNFST QLLDRFLVIA HSYQLNARIL VTKKDKTPIE
KQFEINELLK IYENIGYETE FIGNDDDRKK IVEAWPAGLI VLSGQSGVGK STFLNHYRPE
LNLETNDISK SLNRGKHTTR HVELFERQNG YIADTPGFSA LDFDHIDKDE IKDYFLELNR
YGETCKFRNC NHIKEPNCNV KHQLEIGNIA QFRYDHYLQL FNEISNRKVR Y
