ID A0A1H3MIB2_9RHOB Unreviewed; 352 AA.
AC A0A1H3MIB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05444486_103601 {ECO:0000313|EMBL:SDY75815.1};
OS Lentibacter algarum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lentibacter.
OX NCBI_TaxID=576131 {ECO:0000313|EMBL:SDY75815.1, ECO:0000313|Proteomes:UP000199026};
RN [1] {ECO:0000313|EMBL:SDY75815.1, ECO:0000313|Proteomes:UP000199026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24677 {ECO:0000313|EMBL:SDY75815.1,
RC ECO:0000313|Proteomes:UP000199026};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNPR01000003; SDY75815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3MIB2; -.
DR STRING; 576131.SAMN05444486_103601; -.
DR OrthoDB; 9809485at2; -.
DR Proteomes; UP000199026; 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: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};
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:UP000199026};
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 103..260
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 111..258
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT REGION 326..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 202..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ SEQUENCE 352 AA; 38377 MW; 0879BECBFBBEB3FB CRC64;
MTHDDSEALR PKNAPLSLLQ KLGWGPFFAE QADASVMAET PPVRVTEVHR SGHHVVGEGI
DTILPPRPDA TVGDWILLNA EEPAESVVLE RKNLIKRRAP GPERQVQLIG ANLDTTFIVT
SCNDDFNIAR LERYVALALE DKASPVILLT KADLAEDVES YLSQARSISA DVPVLAIDGR
GEEPRERLAE WCKPGKTVAF IGSSGVGKST LTNTLSGGQE IKTQGIREGD ARGRHTTTSR
QLHLLVSGCT VLDTPGMREV QLTDAASGLG ELFADLQELS TQCRFRDCMH ESEPGCAIKS
ALAAGEIGEA RLERWKKLVA EDAFNSESLS PRRARDRTFG RIAKQPKKKG KK
//