ID E3D6B0_NEIM7 Unreviewed; 307 AA.
AC E3D6B0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=NMBB_0286 {ECO:0000313|EMBL:ADO30801.1};
OS Neisseria meningitidis serogroup B (strain alpha710).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO30801.1, ECO:0000313|Proteomes:UP000006929};
RN [1] {ECO:0000313|EMBL:ADO30801.1, ECO:0000313|Proteomes:UP000006929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX PubMed=20709895; DOI=10.1128/JB.00883-10;
RA Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT "Comparative genome biology of a serogroup B carriage and disease strain
RT supports a polygenic nature of meningococcal virulence.";
RL J. Bacteriol. 192:5363-5377(2010).
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; CP001561; ADO30801.1; -; Genomic_DNA.
DR RefSeq; WP_002218658.1; NC_017505.1.
DR AlphaFoldDB; E3D6B0; -.
DR KEGG; nmp:NMBB_0286; -.
DR PATRIC; fig|630588.3.peg.331; -.
DR HOGENOM; CLU_033617_2_0_4; -.
DR Proteomes; UP000006929; 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: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, ECO:0000313|EMBL:ADO30801.1};
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 85..242
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT DOMAIN 96..240
FT /note="EngC GTPase"
FT /evidence="ECO:0000259|PROSITE:PS50936"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 184..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT BINDING 273
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"
SQ SEQUENCE 307 AA; 33531 MW; 3421C3195FB933CD CRC64;
MPSEHPFSDG ISTPNPKETM NDTAQITASY GRRYIVRTPD GTTYEASTRK KRVDFACGDR
VRISPVNAEQ VVIEDFLPRQ SLLYRQDAWK TKLIAANVTQ LLIVTAAVPS PSMRLLQRAL
LAAEAAGIRA VIVLNKADLP ETALWREKLK FYETLGYPVI ETRALENAGS LRPALQGHSN
ILLGQSGMGK STLTNALLGS QTARTGDISA ALDSGKHTTT HARLYDLNGE TQLIDSPGLQ
EFGLHHLQAA DLPRYFPDFR HLVGQCRFHN CTHRAEPGCA FKAAAQTGAA SPERLAFLQG
ITDELPG
//
