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Database: UniProt
Entry: A0A0M0X7T0_9BACI
LinkDB: A0A0M0X7T0_9BACI
Original site: A0A0M0X7T0_9BACI 
ID   A0A0M0X7T0_9BACI        Unreviewed;       293 AA.
AC   A0A0M0X7T0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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=AMS60_06075 {ECO:0000313|EMBL:KOP82093.1};
OS   Bacillus sp. FJAT-21945.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1581033 {ECO:0000313|EMBL:KOP82093.1, ECO:0000313|Proteomes:UP000036921};
RN   [1] {ECO:0000313|Proteomes:UP000036921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-21945 {ECO:0000313|Proteomes:UP000036921};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Fjat-21945.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of several proteins that assist in the late
CC       maturation steps of the functional core of the 30S ribosomal
CC       subunit. Helps release RbfA from mature subunits. May play a role
CC       in the assembly of ribosomal proteins into the subunit. Circularly
CC       permuted GTPase that catalyzes slow GTP hydrolysis, GTPase
CC       activity is stimulated by the 30S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00711467}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00711466}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00711460}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       RsgA subfamily. {ECO:0000256|SAAS:SAAS00720088}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOP82093.1}.
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DR   EMBL; LITN01000002; KOP82093.1; -; Genomic_DNA.
DR   RefSeq; WP_053475621.1; NZ_LITN01000002.1.
DR   EnsemblBacteria; KOP82093; KOP82093; AMS60_06075.
DR   PATRIC; fig|1581033.3.peg.2437; -.
DR   Proteomes; UP000036921; 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; cd04466; S1_YloQ_GTPase; 1.
DR   CDD; cd01854; YjeQ_EngC; 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   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   Pfam; PF16745; RsgA_N; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00157; TIGR00157; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036921};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00711465};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036921};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720213};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720223};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00720226}.
FT   DOMAIN       63    223       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       72    221       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     112    115       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     166    174       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       247    247       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       252    252       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       254    254       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       260    260       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   293 AA;  33184 MW;  285FEFFF7683E2F8 CRC64;
     MPEGKIIKAL SGFYYVLNES ETVQCRGRGV FRKNKITPLV GDEVVFQAEN DKEGYILEVK
     ERKNELVRPP IANVDQAILV FSAVEPDFST ALLDRFLVLV EFNHIKPIIC ITKMDLTNAK
     QNKEIQHYAE DYRKAGYDVL LTSSETEEGV KELFPYLEGE ISVFAGQSGV GKSSLLNALN
     PDLDLRTDDI SSHLGRGKHT TRHVELIKVG QGLVADTPGF SSLEFMDIEI PDLNFCFPDI
     EKLSEECKFR GCLHMAEPKC AVKAAIENGE LPSYRYEHYK TFLQEIKDRK PRY
//
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