ID A0A1P8WB45_9PLAN Unreviewed; 349 AA.
AC A0A1P8WB45;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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_2 {ECO:0000313|EMBL:APZ91275.1};
GN Synonyms=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN ORFNames=Fuma_00861 {ECO:0000313|EMBL:APZ91275.1};
OS Fuerstiella marisgermanici.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Fuerstiella.
OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ91275.1, ECO:0000313|Proteomes:UP000187735};
RN [1] {ECO:0000313|EMBL:APZ91275.1, ECO:0000313|Proteomes:UP000187735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH11 {ECO:0000313|EMBL:APZ91275.1,
RC ECO:0000313|Proteomes:UP000187735};
RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT Phylum Planctomycetes from the German Wadden Sea.";
RL Front. Microbiol. 7:2079-2079(2016).
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; CP017641; APZ91275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8WB45; -.
DR STRING; 1891926.Fuma_00861; -.
DR KEGG; fmr:Fuma_00861; -.
DR OrthoDB; 9809485at2; -.
DR Proteomes; UP000187735; 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; 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:SF10; SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA; 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, ECO:0000313|EMBL:APZ91275.1};
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:UP000187735};
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 93..251
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 103..249
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT REGION 312..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 194..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 349 AA; 38556 MW; BCC02AB7A3F58E40 CRC64;
MNAQDLRTLG WRPAFQRQLS PEEEQNLIPV RVAAHFGSQV LCLSYSGEFA LPTALIQACG
EVAVGDWLLL EPDSRRGVRR LERESLVARR AAGEKVQRQL IAANLDTLFI VTSCNHDFNL
ARLERYLALA AEAAVEPVVI LTKSDLCDDP LPLRQQAMRL KSGLIVEAID ARDPTQVNSL
ADWCGVAKTV ALVGSSGVGK STLAMTLGVG PLATQEIRED DSRGRHTTTA RHLHRLDAGG
LLIDTPGMRE LQLADCESGL AEVFDDVVAF ADHCRFRNCT HDTEPGCAVQ EAIECGELDK
RRLTSFLKLQ SEEARNSKSL HERRQDSRKQ GQFYKSVMAA KRQRKSGED
//
