RSGA_THEMA
ID RSGA_THEMA Reviewed; 295 AA.
AC Q9X242;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; Synonyms=yjeQ;
GN OrderedLocusNames=TM_1717;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP AND ZINC IONS,
RP AND PROBABLE SUBUNIT.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=15331784; DOI=10.1073/pnas.0405202101;
RA Shin D.H., Lou Y., Jancarik J., Yokota H., Kim R., Kim S.-H.;
RT "Crystal structure of YjeQ from Thermotoga maritima contains a circularly
RT permuted GTPase domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13198-13203(2004).
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 ECO:0000269|PubMed:15331784};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:15331784};
CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000305|PubMed:15331784}.
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; AE000512; AAD36783.1; -; Genomic_DNA.
DR PIR; A72219; A72219.
DR RefSeq; NP_229516.1; NC_000853.1.
DR RefSeq; WP_010865389.1; NC_023151.1.
DR PDB; 1U0L; X-ray; 2.80 A; A/B/C=1-295.
DR PDBsum; 1U0L; -.
DR AlphaFoldDB; Q9X242; -.
DR SMR; Q9X242; -.
DR STRING; 243274.THEMA_05655; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR EnsemblBacteria; AAD36783; AAD36783; TM_1717.
DR KEGG; tma:TM1717; -.
DR PATRIC; fig|243274.18.peg.1092; -.
DR eggNOG; COG1162; Bacteria.
DR InParanoid; Q9X242; -.
DR OMA; CLVAAYD; -.
DR EvolutionaryTrace; Q9X242; -.
DR Proteomes; UP000008183; 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; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding; Zinc.
FT CHAIN 1..295
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000171536"
FT DOMAIN 68..228
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000305|PubMed:15331784"
FT BINDING 170..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000305|PubMed:15331784"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15331784"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15331784"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15331784"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:15331784"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1U0L"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1U0L"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:1U0L"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1U0L"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1U0L"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1U0L"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:1U0L"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:1U0L"
SQ SEQUENCE 295 AA; 33642 MW; E8A9E7396C855848 CRC64;
MNLRRRGIVV SFHSNMVTVE DEETGERILC KLRGKFRLQN LKIYVGDRVE YTPDETGSGV
IENVLHRKNL LTKPHVANVD QVILVVTVKM PETSTYIIDK FLVLAEKNEL ETVMVINKMD
LYDEDDLRKV RELEEIYSGL YPIVKTSAKT GMGIEELKEY LKGKISTMAG LSGVGKSSLL
NAINPGLKLR VSEVSEKLQR GRHTTTTAQL LKFDFGGYVV DTPGFANLEI NDIEPEELKH
YFKEFGDKQC FFSDCNHVDE PECGVKEAVE NGEIAESRYE NYVKMFYELL GRRKK
