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Database: UniProt
Entry: A0A0G0Z3I5_9BACT
LinkDB: A0A0G0Z3I5_9BACT
Original site: A0A0G0Z3I5_9BACT 
ID   A0A0G0Z3I5_9BACT        Unreviewed;       495 AA.
AC   A0A0G0Z3I5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:KKS43302.1};
GN   ORFNames=UV06_C0001G0036 {ECO:0000313|EMBL:KKS43302.1};
OS   Candidatus Collierbacteria bacterium GW2011_GWA2_42_17.
OC   Bacteria; Candidatus Collierbacteria.
OX   NCBI_TaxID=1618378 {ECO:0000313|EMBL:KKS43302.1, ECO:0000313|Proteomes:UP000033854};
RN   [1] {ECO:0000313|EMBL:KKS43302.1, ECO:0000313|Proteomes:UP000033854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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:KKS43302.1}.
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DR   EMBL; LCDA01000001; KKS43302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0Z3I5; -.
DR   PATRIC; fig|1618378.3.peg.36; -.
DR   Proteomes; UP000033854; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; GTP PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          46..146
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   495 AA;  56061 MW;  41D278A078EDDC06 CRC64;
     MEISFEDLLI LAKTKRADIN EARLREVYLF AEKNHAGQIR QTGEGYIIHP LSTAHILASW
     GLDQASLEAA LLHDLPEMAG ITTEELQKNF GEEVVRLIEG VNRVGKVKLR GSQNLQFLEN
     LRRMFVAMAQ DIRVVLIRLA DRLHNISTLD AVPLSKQKRI AIETMEVYAP LAERLGMGRL
     KGDLEDLAFP YIYPDEYTWL QEIAKPHFKY SEKNVSGIMN KLRQQLVKHG IAARVEGRPK
     RKYSLYKKLL RPEINRDISK IYDLMAVRVI TEDTASCYSA LGIIHQYWKP VPNAGISDFI
     AQPKPNGYQS IHTKIFDNMG NIVEIQIRSE EMHLTAELGA AAHFAYSDAK SHGASDEKLT
     AGTAFKISEK MSWVKQLAGW QNQVSTAGDN LEDYKLDALS QHIYVFSPNG DVYDLPENST
     PIDYAFGVHS DLGHYIQTVK INGRIASLDQ PLKSGDIIEV QKSKIMKKPN KNWLRFVKTH
     KAKEEIRKAV QDQPS
//
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