GenomeNet

Database: UniProt
Entry: V6MD25_9BACL
LinkDB: V6MD25_9BACL
Original site: V6MD25_9BACL 
ID   V6MD25_9BACL            Unreviewed;       363 AA.
AC   V6MD25;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   20-DEC-2017, entry version 31.
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=T458_20775 {ECO:0000313|EMBL:EST53283.1};
OS   Brevibacillus panacihumi W25.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Brevibacillus.
OX   NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST53283.1, ECO:0000313|Proteomes:UP000017973};
RN   [1] {ECO:0000313|EMBL:EST53283.1, ECO:0000313|Proteomes:UP000017973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W25 {ECO:0000313|EMBL:EST53283.1,
RC   ECO:0000313|Proteomes:UP000017973};
RX   PubMed=24459276;
RA   Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT   "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT   Halotolerant Hydrocarbon-Degrading Bacterium.";
RL   Genome Announc. 2:e01215-13(2014).
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   -!- 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|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:EST53283.1}.
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; AYJU01000017; EST53283.1; -; Genomic_DNA.
DR   EnsemblBacteria; EST53283; EST53283; T458_20775.
DR   PATRIC; fig|1408254.3.peg.4070; -.
DR   Proteomes; UP000017973; 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:UP000017973};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820};
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:UP000017973};
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      111    270       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      121    268       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     160    163       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     212    220       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   COILED      325    345       {ECO:0000256|SAM:Coils}.
FT   METAL       293    293       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       298    298       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       300    300       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       306    306       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   363 AA;  40558 MW;  74200237C6F23D3D CRC64;
     MNQPQQENKA ERILQKMGWN AAFEAHFAPY AEQGYSVGRV TLEHKRIYRV ISEHGELLGE
     VTGKLRYEAS GREDYPAVGD WVVISPRPEE QKATIHALLP RKSKFSRKVA GSTVEEQIVA
     TNVDTVFLVN ALNHDFNLRR IERYLILAWE SGAAPVIVLS KADLCDDLEA RIAEVESVAI
     GVPVHVVSAE QDEGLDQLAP YLGEGQTVAL LGSSGVGKST LINKLSGAEM QRVSEVRAGD
     DRGRHTTTHR ELFLLPRGGL MIDTPGMREL QLWEADEGFR DAFDDIESLG ESCRFSDCQH
     LREPGCAIRA ALADGTLDQS RYDNYRKLQR ELAHLARKED AALRAAEKAK WKKITMGQRQ
     KKK
//
DBGET integrated database retrieval system