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Database: UniProt
Entry: E6WG01_PANSA
LinkDB: E6WG01_PANSA
Original site: E6WG01_PANSA 
ID   E6WG01_PANSA            Unreviewed;       353 AA.
AC   E6WG01;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN   OrderedLocusNames=Pat9b_3566 {ECO:0000313|EMBL:ADU70856.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU70856.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU70856.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU70856.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01820}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01820};
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01820}.
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DR   EMBL; CP002433; ADU70856.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6WG01; -.
DR   STRING; 592316.Pat9b_3566; -.
DR   KEGG; pao:Pat9b_3566; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_0_6; -.
DR   Proteomes; UP000001624; 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; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00157; ribosome small subunit-dependent GTPase A; 1.
DR   PANTHER; PTHR32120; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 1.
DR   PANTHER; PTHR32120:SF11; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01820}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01820}; Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   DOMAIN          104..276
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          121..274
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..163
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         214..222
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   353 AA;  39150 MW;  6DB143675A3EB930 CRC64;
     MRGCVSKNKL SKGQQRRVSA NHERRLKQRN EKPEPDDSLF GEPTDGVVIS RFGMHADVED
     SSGEVHRCNI RRTIRSLVTG DRVVWRAANE NGGKGIVEAV YDRTSVLTRP DFYDGVKPIA
     ANIDQIIIVS AILPELSLNI IDRYLVASET LGIEPLLVLN KTDLLDDDAR AFVDEQMEIY
     RHIGYRVLMV SSRAKNGLDE LEAALTGRIS IFAGQSGVGK SSLLNALLGL DVAGDEILTN
     DVSDVSGLGQ HTTTAARLYH FPHGGDVIDS PGVREFGLWH LEPEQITRGF VEFREFLGDC
     KFRDCKHGND PGCAIREAVD NGTIDVSRFD NYHRILESMA QVKTRKNFSA SED
//
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