ID A0A1G1ZBK4_9BACT Unreviewed; 566 AA.
AC A0A1G1ZBK4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ACT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3H06_01810 {ECO:0000313|EMBL:OGY61904.1};
OS Candidatus Colwellbacteria bacterium RIFCSPLOWO2_12_FULL_44_13.
OC Bacteria; Candidatus Colwellbacteria.
OX NCBI_TaxID=1797694 {ECO:0000313|EMBL:OGY61904.1, ECO:0000313|Proteomes:UP000176976};
RN [1] {ECO:0000313|EMBL:OGY61904.1, ECO:0000313|Proteomes:UP000176976}
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:OGY61904.1}.
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DR EMBL; MHJC01000006; OGY61904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZBK4; -.
DR Proteomes; UP000176976; 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; 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;
FT DOMAIN 37..135
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 381..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 491..566
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 566 AA; 65222 MW; 14BA76AA91ADEC1E CRC64;
MTIEELIKTQ PHSLSRRAYD FAFKVHRGQK RLSGEPYFNH VVGTAQSLLD WRLDEVSIAA
GLLHDVVEDS DYTIEDLQKE FGDEVAFLVD GVTKLGRLKY RGAERQVESL RKMILALSQD
LRVVLIKLAD RLYNMRTLDA LPPHKQKRIA LETSEIYAPL AYRLGMQRLS GELQDLAFPY
LYPQEHTWLR EQVKNRYHIR EAYLRRIAPK VEEALKEASI DILNIDFRAK RYSSLYKKLL
RYEMDVDKIH DLIAFRIVVT SLPDCYNALG IIHQLFPPVP GRIKDYIALP KPNGYQSIHT
TVFGPEQRAI EFQIRTQEMH DEAENGIAAH WAYEQTKGTG AYVKRTSSFA DMNDITWVHQ
LRSWQEKFAD SEEFIESLKV DFFKDRIFCL TPQGEVVDLP LGSTPVDFAY QIHSEIGNQC
VGARVNQKFV PLDYELSSSD VVEIAIQKNK KPSVSWLNFV KTSNARDHIR AVLRSSRSQN
GLLRQAARES ELRLTVYDRP GLLRDIVETI SRSHVNVLSV TTNPISKSRL QLFKIKCNTV
NKEKLQKLLL KLKGTKEVKE TSYLLS
//