ID   A0A432Q1C2_9AQUI        Unreviewed;       295 AA.
AC   A0A432Q1C2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   11-DEC-2019, entry version 6.
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:RUM32051.1};
GN   ORFNames=DSY42_01770 {ECO:0000313|EMBL:RUM32051.1};
OS   Aquifex sp.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex;
OC   unclassified Aquifex.
OX   NCBI_TaxID=313370 {ECO:0000313|EMBL:RUM32051.1, ECO:0000313|Proteomes:UP000287362};
RN   [1] {ECO:0000313|EMBL:RUM32051.1, ECO:0000313|Proteomes:UP000287362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAG 11 {ECO:0000313|EMBL:RUM32051.1};
RA   Trembath-Reichert E., Huber J.A.;
RT   "Combined omics and stable isotope probing to characterize newly discovered
RT   Mariana Back-Arc vent microbial communities.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of several proteins that assist in the late maturation
CC       steps of the functional core of the 30S ribosomal subunit. Helps
CC       release RbfA from mature subunits. May play a role in the assembly of
CC       ribosomal proteins into the subunit. Circularly permuted GTPase that
CC       catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S
CC       ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01820}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {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. RsgA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00535129}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUM32051.1}.
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DR   EMBL; QNXQ01000037; RUM32051.1; -; Genomic_DNA.
DR   Proteomes; UP000287362; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00064626};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00211110};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00211158};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00447475};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS01203909};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS01203910};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS01203911};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00211157}.
FT   DOMAIN          64..224
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   DOMAIN          73..222
FT                   /note="EngC GTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS50936"
FT   NP_BIND         113..116
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   NP_BIND         167..175
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   METAL           247
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   METAL           252
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   METAL           254
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
FT   METAL           260
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01820"
SQ   SEQUENCE   295 AA;  34138 MW;  5B892DEA58EB7549 CRC64;
     MKRAIVIDRE AQMIEVYTLD DKETYRGIPR GKVLKKTKIY AGDYVWGEVI DKNTFAIEEV
     EERKNLLIRP RVANVNRIIV VQTLKMPEFN NYLLDNLLVV YEYFGVEPVI VFNKVDILDE
     EERKELDYWI NIYKNAGYDV LKVSAKLSEG IDNLVNYLEG FICILAGPSG VGKSSILSKL
     TGTQLRTQEV SEKTERGRHT TTGVRLIPFG KGSFIGDTPG FSKVEATMFI KWREIRKYFR
     EFLAYQCKYP DCTHTNEPEC AVKEAVKEGE ISCERYKSYL KMIKVYLEDI KELCK
//