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Database: UniProt
Entry: A0A0F2CDZ4_9MICO
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ID   A0A0F2CDZ4_9MICO        Unreviewed;       355 AA.
AC   A0A0F2CDZ4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 18.
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   ECO:0000313|EMBL:KJQ55875.1};
GN   ORFNames=RS85_00249 {ECO:0000313|EMBL:KJQ55875.1};
OS   Microbacterium sp. SA39.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ55875.1, ECO:0000313|Proteomes:UP000033425};
RN   [1] {ECO:0000313|EMBL:KJQ55875.1, ECO:0000313|Proteomes:UP000033425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA39 {ECO:0000313|EMBL:KJQ55875.1,
RC   ECO:0000313|Proteomes:UP000033425};
RA   Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N.,
RA   Brader G.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on
RT   heavy metal contaminated environments.";
RL   Submitted (JAN-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:SAAS00828801}.
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|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:KJQ55875.1}.
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DR   EMBL; JXRU01000020; KJQ55875.1; -; Genomic_DNA.
DR   RefSeq; WP_046011604.1; NZ_JXRU01000020.1.
DR   EnsemblBacteria; KJQ55875; KJQ55875; RS85_00249.
DR   PATRIC; fig|1263625.4.peg.260; -.
DR   Proteomes; UP000033425; 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:UP000033425};
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:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101, ECO:0000313|EMBL:KJQ55875.1};
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:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033425};
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      122    279       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      131    277       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     171    174       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     218    226       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       303    303       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       307    307       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       309    309       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       316    316       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   355 AA;  38344 MW;  DBD11E7B3DEB9186 CRC64;
     MSWLDDSDLE DDFEDFDESS IRTRPNPKAN RPRTKRRPAH EDAQNGRVLG VDRGRYTVLM
     DEDTEDEHII SAVRARELRR MPIVTGDQAR VVGDTSGDEG TLSRIIGIAD RTSLLRRSAD
     DTDQVERVIV ANADQMLVVV AAADPEPRAR LVDRYLVAAL DAGIRPLLVV TKTDIADPTA
     FLTHFDGLDL QVFTSAQDEM PIDEIGAALV GRSTVFVGHS GVGKSTLVNE LVPSAGRATG
     HVNQVTGRGR HTSSSTVSLR YHGVLGTGWV IDTPGVRSFG LGHVDPANIL AAFTELAAIA
     ENCPRGCTHL ADAPDCALIE AAERGELGET GRARLDSLQR LLQTFADKAD QAPGR
//
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