ID   A0A432Q1C2_9AQUI        Unreviewed;       295 AA.
AC   A0A432Q1C2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-NOV-2019, entry version 5.
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
RT   discovered 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
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01820};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       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|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00535129}.
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: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   Complete proteome {ECO:0000313|Proteomes:UP000287362};
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,
KW   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       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN       73    222       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     113    116       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     167    175       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       247    247       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       252    252       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       254    254       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       260    260       Zinc. {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
//