GenomeNet

Database: UniProt
Entry: K9F2C2_9ACTO
LinkDB: K9F2C2_9ACTO
Original site: K9F2C2_9ACTO 
ID   K9F2C2_9ACTO            Unreviewed;       335 AA.
AC   K9F2C2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
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=HMPREF9233_00417 {ECO:0000313|EMBL:EKU95630.1};
OS   Actinobaculum massiliense ACS-171-V-Col2.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinobaculum.
OX   NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95630.1, ECO:0000313|Proteomes:UP000009888};
RN   [1] {ECO:0000313|EMBL:EKU95630.1, ECO:0000313|Proteomes:UP000009888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B.,
RA   Vaneechoutte M., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL   Submitted (SEP-2012) 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:EKU95630.1}.
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; AGWL01000002; EKU95630.1; -; Genomic_DNA.
DR   RefSeq; WP_007000635.1; NZ_JH992955.1.
DR   EnsemblBacteria; EKU95630; EKU95630; HMPREF9233_00417.
DR   PATRIC; fig|883066.3.peg.437; -.
DR   OrthoDB; POG091H01WX; -.
DR   Proteomes; UP000009888; 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:UP000009888};
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};
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:UP000009888};
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       97    267       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      116    265       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     156    159       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     209    217       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       291    291       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       295    295       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       297    297       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       304    304       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   335 AA;  36421 MW;  06A39D92E59F9A52 CRC64;
     MRDIGTDDPR VHVRPGRPSK PRTKIRPDYS DRPRGQVITV DRGRYGVVMD DAVEVIAVKA
     RELGRGALVV GDRVRLTGDL SGRKDTLARI VLIEERRTEL TRSTDEGGGR ERTIVANADQ
     MAIVVALAQP EPKFGMIDRA LVAAMEAGMQ PLLVLTKADL ASHQKVEEVY EPLGLRVFVT
     AVKHPAAPQR DDLEALREAL TGHDTVLIGH SGVGKSTLFN TLVPDADRRT GDVNDVTGKG
     RHTSVNAVSF ALPGGGRIID TPGVRSFGLA HVDAAGLLRG FPDLEEVTAD CPRGCTHKAN
     ETECALDTVR DPLGQRRVES LRRLLEQVPK PEWEG
//
DBGET integrated database retrieval system