GenomeNet

Database: UniProt
Entry: A0A0U2W853_9BACL
LinkDB: A0A0U2W853_9BACL
Original site: A0A0U2W853_9BACL 
ID   A0A0U2W853_9BACL        Unreviewed;       302 AA.
AC   A0A0U2W853;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=IJ22_11860 {ECO:0000313|EMBL:ALS21562.1};
OS   Paenibacillus naphthalenovorans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS21562.1, ECO:0000313|Proteomes:UP000061660};
RN   [1] {ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic
RT   Paenibacillus species.";
RL   Submitted (DEC-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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013652; ALS21562.1; -; Genomic_DNA.
DR   RefSeq; WP_062407880.1; NZ_CP013652.1.
DR   EnsemblBacteria; ALS21562; ALS21562; IJ22_11860.
DR   KEGG; pnp:IJ22_11860; -.
DR   PATRIC; fig|162209.4.peg.1261; -.
DR   KO; K06949; -.
DR   Proteomes; UP000061660; 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; 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:UP000061660};
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:UP000061660};
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       67    232       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       76    230       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     116    119       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     174    182       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       256    256       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       261    261       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       263    263       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       269    269       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   302 AA;  33005 MW;  8D3B7D15424AEC47 CRC64;
     MPTGFIVKAL SGYYYVLPED SQSAESIQCR ARGIFKKRGI SPLVGDRVIY QLTENGEGTV
     DEILPRTSEL VRPPVANVDL VVLVFSVDEP ALNLPLLDKF LVHTESAGLD ALICLTKHDL
     LADSREHGGP LELESVIKLY ESIGYTILVT SAKEGVGVDK VMDQLSGRIS VFAGQSGVGK
     SSLLNAMVPG LQLETNQISM KLGRGKHTTR HVELIRLQNG GIVADTPGFS QLDFLQVDAE
     GLGGCFREFA PFAAECRFRG CLHLHEPGCK VQEAADAGLI AATRYENYLQ FLGEIRDKKR
     RY
//
DBGET integrated database retrieval system