ID A0A1F6BTV4_9BACT Unreviewed; 564 AA.
AC A0A1F6BTV4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=TGS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2116_01665 {ECO:0000313|EMBL:OGG40374.1};
OS Candidatus Jorgensenbacteria bacterium GWA1_49_17.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1798467 {ECO:0000313|EMBL:OGG40374.1, ECO:0000313|Proteomes:UP000179368};
RN [1] {ECO:0000313|EMBL:OGG40374.1, ECO:0000313|Proteomes:UP000179368}
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:OGG40374.1}.
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DR EMBL; MFKG01000017; OGG40374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6BTV4; -.
DR Proteomes; UP000179368; Unassembled WGS sequence.
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; 3.30.70.260; -; 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; 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; PF01842; ACT; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 382..445
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 488..563
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 564 AA; 65426 MW; 6CFA7BD74C006AC4 CRC64;
MDTGWLQKYP QKSSVREAFD FAKEAHKDKK RNSGEPYFSH CEAVAETVSE WGLDDESVAA
ALLHDVIEDT SYTLRDIEKR FGKEIASIVD GLTKLDKVPF PEKDQNVETL RKFIISFSRD
LRVVIVKLAD RHHNMFTLKF LPPERQKSFA WETSEIYAPL AYRLGMQRLS GELEDLTFPF
LHPEEYKWLL KNVKVKFEER EKYAEELKPL VKKLLLKNSI RPIAVDSRAK RYSSLYKKLH
RHDMDFEKIY DLVALRIVVK TVEDCYATLG IIHKIWPPLP GRIKDYIARP KPNGYRSLHT
TVFAGDNKIT EFQIRTEEMH REDELGIAAH WAYEQVKGSK RNGRNWRGVR NHKELLWVEQ
LRSWQQNISD KDFVDSLAVD FFKERIFVIT PHNDVIDLPH GATPVDFAYH IHSEIGNQCV
GAKVNGKIVP LDYELRSGDM VEIMTQRGKN PSEGWLRFIK TSLARDQIKG MIRKVTRFPA
SREPESTEFK IVNRDRPGFL KDVTGEFSAM KINITYLQSS TDKRGVLSTV TVRTEPLSKT
KIEKLLVKIK SVEGVKEVSS KFNR
//
