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Database: UniProt
Entry: Z9JPR9_9MICO
LinkDB: Z9JPR9_9MICO
Original site: Z9JPR9_9MICO 
ID   Z9JPR9_9MICO            Unreviewed;       348 AA.
AC   Z9JPR9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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   ORFNames=BF93_10040 {ECO:0000313|EMBL:EWS79752.1};
OS   Brachybacterium phenoliresistens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS79752.1, ECO:0000313|Proteomes:UP000023067};
RN   [1] {ECO:0000313|EMBL:EWS79752.1, ECO:0000313|Proteomes:UP000023067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W13A50 {ECO:0000313|EMBL:EWS79752.1,
RC   ECO:0000313|Proteomes:UP000023067};
RA   Wang X.;
RT   "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWS79752.1}.
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DR   EMBL; JDYK01000026; EWS79752.1; -; Genomic_DNA.
DR   RefSeq; WP_038374433.1; NZ_KK070008.1.
DR   AlphaFoldDB; Z9JPR9; -.
DR   STRING; 396014.BF93_10040; -.
DR   PATRIC; fig|396014.3.peg.3501; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_1_0_11; -.
DR   OrthoDB; 9809485at2; -.
DR   Proteomes; UP000023067; Unassembled WGS sequence.
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; 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; 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|HAMAP-Rule:MF_01820};
KW   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}; Reference proteome {ECO:0000313|Proteomes:UP000023067};
KW   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          115..274
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          124..272
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..167
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         215..223
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   348 AA;  37358 MW;  0156C36DD414107E CRC64;
     MVGRRSRDWD ESDVRVRPNR RGSRPRTKDR PAHRDAVPAR VVAVDRGRWR TVVDEGGAQE
     RAVTAMRARE LGRSPVVPGD VVALAGDVSG REGTLARIVR IEERSSFLRR SADDDDATER
     PLVANVDLMV MVTALADPEP RGGMIDRCLV AAYVAGVDAL LVLTKADLRS PAPFLETYAP
     LGLEHVVTSR REDGGITGLD PLREHLDGRI SVLIGHSGVG KSTLLNALVP GADRATGAVN
     DVTGRGRHTS SSALALRLPS HDGWLIDTPG VRSFGLGHVD PEDLLDAFAD LAPLAEECPR
     GCTHLEDAPD CSLDAAVAAG RAGTAGPSRL ESYRRLATAL RRNDPWDL
//
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