ID A0A1F8RT57_9CHLR Unreviewed; 733 AA.
AC A0A1F8RT57;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:OGO50843.1};
GN ORFNames=A2148_03945 {ECO:0000313|EMBL:OGO50843.1};
OS Chloroflexi bacterium RBG_16_68_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797660 {ECO:0000313|EMBL:OGO50843.1, ECO:0000313|Proteomes:UP000176790};
RN [1] {ECO:0000313|EMBL:OGO50843.1, ECO:0000313|Proteomes:UP000176790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGO50843.1}.
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DR EMBL; MGOB01000065; OGO50843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RT57; -.
DR STRING; 1797660.A2148_03945; -.
DR Proteomes; UP000176790; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 51..156
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 400..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 652..726
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 499..526
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 733 AA; 83494 MW; 96F196EA0AEC83FB CRC64;
MAQAREKEGL QHLLEQARGY LPEDRIRLIE EAYAFAESCH ADQRRESGEP FIVHPLDAAL
TIASLQLDAD AVAAALLHDV QEDCDVPNQE LKRRFGAEVA KLVDGVTKLK RIAWQSPEPG
IVDGAMQAEN LRKMLLAMAE DVRVVIIKLA DRLHNMRTLE HLEAAKRLST AQETMEIYAP
LAGRLGIWQM KWELEDLAFC HLQPEKYQEI AQLIASRRTT RERYIAQVEK ILREELTKQG
VEAAIQGRAK HIYSVYQKMQ KYGDQGKTFN EIYDLLALRV LVNTVTDCYG ALGAVHGLWR
PIPGQFDDYI ANPKEGVYQS LHSTVMCLGA RPLEVPIRTH EMHRLAEYGV AAHWRYKEGG
RQDVRFEERL SWLRQLLEWQ RDMAHAEEFV ETVKTDVFQD QVFVYTPKGE IKDLPAGSTP
IDFAYRIHTD LGQHCIGAKV NGRLVALNQP LENGDVVEIL VGRSSRGPSR DWLNRNLGYV
QTSHARQKIR QWFRKQERAE NIEKGREMLE KELRRLGLTM ARCKDELLRQ SRYDTLDDLY
AALGFGGASL HQVAVRLERF LKPQEPEPPT EGEAPRRAVS ATGIQVLGTG DLLTQLARCC
NPVLGDEIIG YVTRSRGVTI HRRDCFNVLH EDERQRLVEV EWGRSGDLYP VAVNIEAWDR
VGLLRDISTI IAEEKVNMVA VRTQEREDRT TCISLTLETQ GVNQLSRLLS KLETVRGVTS
VSRSLNQARE RLS
//
