RSGA_SALTY
ID RSGA_SALTY Reviewed; 350 AA.
AC Q8ZKB0;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 114.
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=engC, yjeQ;
GN OrderedLocusNames=STM4349;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-350 IN COMPLEX WITH GDP AND
RP ZINC IONS, AND PROBABLE SUBUNIT.
RX PubMed=18007041; DOI=10.1107/s1744309107048609;
RA Nichols C.E., Johnson C., Lamb H.K., Lockyer M., Charles I.G.,
RA Hawkins A.R., Stammers D.K.;
RT "Structure of the ribosomal interacting GTPase YjeQ from the
RT enterobacterial species Salmonella typhimurium.";
RL Acta Crystallogr. F 63:922-928(2007).
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:18007041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:18007041};
CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000305|PubMed:18007041}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL23172.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL23172.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_463213.3; NC_003197.2.
DR PDB; 2RCN; X-ray; 2.25 A; A=2-350.
DR PDBsum; 2RCN; -.
DR AlphaFoldDB; Q8ZKB0; -.
DR SMR; Q8ZKB0; -.
DR IntAct; Q8ZKB0; 1.
DR STRING; 99287.STM4349; -.
DR PaxDb; Q8ZKB0; -.
DR EnsemblBacteria; AAL23172; AAL23172; STM4349.
DR GeneID; 1255875; -.
DR KEGG; stm:STM4349; -.
DR PATRIC; fig|99287.12.peg.4576; -.
DR HOGENOM; CLU_033617_2_0_6; -.
DR OMA; CLVAAYD; -.
DR PhylomeDB; Q8ZKB0; -.
DR EvolutionaryTrace; Q8ZKB0; -.
DR Proteomes; UP000001014; 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 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..350
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000008157"
FT DOMAIN 104..273
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000305|PubMed:18007041"
FT BINDING 214..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000305|PubMed:18007041"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:18007041"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:18007041"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:18007041"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820,
FT ECO:0000269|PubMed:18007041"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2RCN"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:2RCN"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2RCN"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2RCN"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:2RCN"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:2RCN"
SQ SEQUENCE 350 AA; 38948 MW; FC0E9580E7028405 CRC64;
MSKNKLSKGQ QRRVNANHQR RLKTSAEKAD YDDNLFGEPA EGIVISRFGM HADVESADGE
VHRCNIRRTI RSLVTGDRVV WRPGKAAAEG VNVKGIVEAV HERTSVLTRP DFYDGVKPIA
ANIDQIVIVS AILPELSLNI IDRYLVGCET LQVEPLIVLN KIDLLDDEGM DFVNEQMDIY
RNIGYRVLMV SSHTQDGLKP LEEALTGRIS IFAGQSGVGK SSLLNALLGL QNEILTNDVS
NVSGLGQHTT TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGHCKYR
DCKHDADPGC AIREAVENGA IAETRFENYH RILESMAQVK TRKNFSDTDD
