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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//