ID A0A1F8B2S6_9BACT Unreviewed; 502 AA.
AC A0A1F8B2S6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=TGS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2955_01115 {ECO:0000313|EMBL:OGM58230.1};
OS Candidatus Woesebacteria bacterium RIFCSPLOWO2_01_FULL_37_19.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802514 {ECO:0000313|EMBL:OGM58230.1, ECO:0000313|Proteomes:UP000177501};
RN [1] {ECO:0000313|EMBL:OGM58230.1, ECO:0000313|Proteomes:UP000177501}
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:OGM58230.1}.
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DR EMBL; MGHA01000048; OGM58230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8B2S6; -.
DR STRING; 1802514.A2955_01115; -.
DR Proteomes; UP000177501; 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; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; 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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 51..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..467
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 502 AA; 57207 MW; F96D7414712712BB CRC64;
MKSKPDLKFS ELIADYKSYM DNKSDTRLLK KAWDFAKLAH TGQKRLTGVP YVNHPLETAK
ILTSWKLDAA TIAAGLLHDT VEDGGATEED LIKEFGIEIS QLVAGVTKVS NVKLRGSKDQ
EFVENLRKMF LAMAKDLRVV LVKLADRMHN MRTLYAIPKE KQERIARETL EVFAPLAERL
GMGEVKAKLD DLAFPYVYQE KYKLVKKESL IHYKKAEETI KTMKRAILRR AAELEVKVRV
NGRKKHLYSL WLKLERPEIS WDFEKIHDIV ALRVLVDSVA ECYTALGVIH NLYKPVPHLG
VSDFIAQPKP NGYQSIHTKV FGPKGKIVEV QIRTYEMHES AEYGIASHWA YSQAKSRGIS
GELLENRGVA VDSEKLSWVK QLADWQKELA DSEEFLRAVK FDALSHRNFV FSPLGDVYNL
PKGSTPVDFA YAVHTQLGSY IKGVKVDGKV VPLDFKLRSG QVVEIIKSKS SHPPRSDWLK
FVVTTTARKE INKYLRNLRI KE
//
