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Database: UniProt
Entry: Q4A6T0_MYCS5
LinkDB: Q4A6T0_MYCS5
Original site: Q4A6T0_MYCS5 
ID   Q4A6T0_MYCS5            Unreviewed;       276 AA.
AC   Q4A6T0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 109.
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=MS53_0120 {ECO:0000313|EMBL:AAZ43541.2};
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ43541.2, ECO:0000313|Proteomes:UP000000549};
RN   [1] {ECO:0000313|EMBL:AAZ43541.2, ECO:0000313|Proteomes:UP000000549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53 {ECO:0000313|EMBL:AAZ43541.2,
RC   ECO:0000313|Proteomes:UP000000549};
RX   PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA   Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O.,
RA   Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L.,
RA   Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M.,
RA   Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M.,
RA   de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G.,
RA   Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A.,
RA   Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.,
RA   Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I.,
RA   Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R.,
RA   Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C.,
RA   Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H.,
RA   Zuccherato L.W., Simpson A.J., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
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; AE017245; AAZ43541.2; -; Genomic_DNA.
DR   RefSeq; WP_011283284.1; NC_007294.1.
DR   AlphaFoldDB; Q4A6T0; -.
DR   STRING; 262723.MS53_0120; -.
DR   GeneID; 61970341; -.
DR   KEGG; msy:MS53_0120; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_1_14; -.
DR   OrthoDB; 9809485at2; -.
DR   Proteomes; UP000000549; 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};
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:UP000000549};
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          57..211
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          66..209
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   BINDING         106..109
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         155..163
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   276 AA;  31944 MW;  7402551D87992AAC CRC64;
     MNRVFELFGQ TANVCDLENN CKLLPFAGRL KKLKITPKVG DIVEVENDLI TDIKPRKNEL
     IRPKVANIDQ VLVFLSVKEP DFSSFLLDKY LAIVESKNID LIIFLTKSDL DLELANHWKQ
     KYEMQNYKVF LLSSNDNNYD EIKKLFDKKF SIVMGQSGVG KTTFINNISN NNYKTQQISK
     SLSRGKHTTT SAKIISFLNG FLIDSPGFSS LDVEKEINLN KSYLNFKELA KLCEFKDCMH
     NFEKNCNVKL NLNSNLVPEF RYKNYLKLLK EQNERK
//
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