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Database: UniProt
Entry: A0A0R2EQ61_9LACO
LinkDB: A0A0R2EQ61_9LACO
Original site: A0A0R2EQ61_9LACO 
ID   A0A0R2EQ61_9LACO        Unreviewed;       356 AA.
AC   A0A0R2EQ61;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-DEC-2018, entry version 19.
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=FD14_GL002073 {ECO:0000313|EMBL:KRN18209.1};
OS   Lactobacillus similis DSM 23365 = JCM 2765.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN18209.1, ECO:0000313|Proteomes:UP000051442};
RN   [1] {ECO:0000313|EMBL:KRN18209.1, ECO:0000313|Proteomes:UP000051442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN18209.1,
RC   ECO:0000313|Proteomes:UP000051442};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(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, ECO:0000256|SAAS:SAAS00828801}.
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       ECO:0000256|SAAS:SAAS00828796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00820346}.
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:KRN18209.1}.
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DR   EMBL; AYZM01000158; KRN18209.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRN18209; KRN18209; FD14_GL002073.
DR   PATRIC; fig|1423804.4.peg.2254; -.
DR   Proteomes; UP000051442; 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; 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; 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:UP000051442};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00820338};
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};
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   Reference proteome {ECO:0000313|Proteomes:UP000051442};
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      103    258       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      109    256       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     148    151       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     200    208       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       279    279       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       284    284       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       286    286       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       292    292       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   356 AA;  38309 MW;  2EC6F50BC1B21E1A CRC64;
     MNFKPLTLSQ LGASSELAAQ LTSSLSLGRV ISVNRTLLTV AADEKIAQAT LAGRLLNTAF
     EAEDYPTVGD WVGLREVADT AVIERLLPRQ SLLMRKAAGR TSSAQLIAAN VDVLLICMAL
     DQNFNLRRLE RYLSLAHASG ALATVVLTKA DQASDLENQL LTVNAIAGSS PVVVCNAVAA
     DGLRSLEQLL KPQLTYALIG SSGVGKSTLI NRLLGNGTLA TQAVRQSDAH GRHTTTGRDL
     FQLPTGSLVI DTPGMRELGL LDADVDATFQ DILALVVNCK FNNCTHTHEP GCAVQAAVNT
     GQLDAQRLRN YQQLTDEQAE NTALRGRARE EAKINRMFGS KKAMKTAMQQ ARRKRH
//
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