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Database: UniProt
Entry: E6SJB0_THEM7
LinkDB: E6SJB0_THEM7
Original site: E6SJB0_THEM7 
ID   E6SJB0_THEM7            Unreviewed;       303 AA.
AC   E6SJB0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Tmar_0924 {ECO:0000313|EMBL:ADU51038.1};
OS   Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS   7p75a).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX   NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51038.1, ECO:0000313|Proteomes:UP000008915};
RN   [1] {ECO:0000313|EMBL:ADU51038.1, ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   PubMed=21304738;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75a).";
RL   Stand. Genomic Sci. 3:337-345(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   DOI=10.4056/sigs.1373474;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA   Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75aT).";
RL   Stand. Genomic Sci. 3:337-345(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; CP002344; ADU51038.1; -; Genomic_DNA.
DR   RefSeq; WP_013495343.1; NC_014831.1.
DR   AlphaFoldDB; E6SJB0; -.
DR   STRING; 644966.Tmar_0924; -.
DR   KEGG; tmr:Tmar_0924; -.
DR   eggNOG; COG1162; Bacteria.
DR   HOGENOM; CLU_033617_2_1_9; -.
DR   OrthoDB; 9809485at2; -.
DR   Proteomes; UP000008915; 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; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   InterPro; IPR031944; RsgA_N.
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   Pfam; PF16745; RsgA_N; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01820};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01820};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01820};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01820}; Reference proteome {ECO:0000313|Proteomes:UP000008915};
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          66..231
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          75..229
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   BINDING         115..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         173..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   303 AA;  33039 MW;  410F1511EA8F53A3 CRC64;
     MPARTGTVVK AQTNLYEVRL DDTGEVLLCA LRGRLRRQAG DVLTGDRVEV VLQPGGAAIE
     RVLPRRNRLV RPPIANVDRV LLIQSLADPD PVPILMDRVL VQAEALELPV VLCFTKLDLV
     VKSPDDPLPE PSARLVDGYR RAGYPVHLVA APRGWGLDAL AAALKEGATV LAGPSGAGKS
     TLLNALQPGL QLATGEVSRK LGRGRHTTRH VALLPLAEGG WVADTPGFSR VDLPDLEPEE
     LGDLWPEIRR EAPDCRFRGC LHRSEPGCAV RAARDAGRIA AWRYQNYLVL LGELEERLAE
     RYK
//
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