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Database: UniProt
Entry: A0A124F6U1_9GAMM
LinkDB: A0A124F6U1_9GAMM
Original site: A0A124F6U1_9GAMM 
ID   A0A124F6U1_9GAMM        Unreviewed;       339 AA.
AC   A0A124F6U1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-DEC-2018, entry version 14.
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=XD36_0068 {ECO:0000313|EMBL:KUJ89445.1};
OS   Halomonas sp. 54_146.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ89445.1, ECO:0000313|Proteomes:UP000053192};
RN   [1] {ECO:0000313|EMBL:KUJ89445.1, ECO:0000313|Proteomes:UP000053192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54_146 {ECO:0000313|EMBL:KUJ89445.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
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}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       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.
CC       RsgA subfamily. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       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:KUJ89445.1}.
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DR   EMBL; LGEN01000001; KUJ89445.1; -; Genomic_DNA.
DR   PATRIC; fig|1635257.4.peg.71; -.
DR   Proteomes; UP000053192; 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   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   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053192};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00087595};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101, ECO:0000313|EMBL:KUJ89445.1};
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:SAAS00064566};
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      112    274       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      120    272       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     159    162       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     212    220       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   COILED       16     36       {ECO:0000256|SAM:Coils}.
FT   METAL       298    298       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       303    303       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       305    305       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       311    311       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   339 AA;  37458 MW;  FC0BB1ED940CB9CD CRC64;
     MSKRKLSRQQ QWRVEKVQAE RAQRAEKRDV QDAEKLAAGE YGAEQPGRVV AHFGRTLEVR
     NSNNEPVRCH LRANLDGLVT GDRVIWRAGQ EGSGVVVARE ERDSVLKRPD ARGLLKPVAA
     NIDQLLIVFA VEPAPHANLI DRYLVAAEAT GIAPVLVLNK TDLLPEDGGE LGKLLERYRA
     LGYPVVRTTT ATENGLDELR SQLEGRTSVF VGQSGVGKSS LIDLLLPDET LRIGALSEDS
     RKGTHTTTTA RLYTMSRAEV ADGDLIDSPG IREFGLVHLN EQEVTDGFIE FHDYIGHCRF
     RDCRHRNEPG CALLAAVEAG KIHPARFASY RRILDSLDS
//
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