ID A0A1G0T966_9BACT Unreviewed; 723 AA.
AC A0A1G0T966;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:OGU81200.1};
GN ORFNames=A2W11_08290 {ECO:0000313|EMBL:OGU81200.1};
OS Ignavibacteria bacterium RBG_16_35_7.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798434 {ECO:0000313|EMBL:OGU81200.1, ECO:0000313|Proteomes:UP000178403};
RN [1] {ECO:0000313|EMBL:OGU81200.1, ECO:0000313|Proteomes:UP000178403}
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:OGU81200.1}.
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DR EMBL; MHAG01000135; OGU81200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0T966; -.
DR Proteomes; UP000178403; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
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; IPR045600; RelA/SpoT_AH_RIS.
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; PF19296; RelA_AH_RIS; 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 53..152
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 396..457
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 648..722
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 723 AA; 82981 MW; ACF72DF698166609 CRC64;
MNFNNPKYNK MFDRLLEACE RNFPSTDEKF LAKGFEFAIE AHKNDRRASG DEYITHPFEV
ALIVAQEIPL DEVTVVSALL HDTIEDTEIS VELLQKEFGK EVAEIVDGVT KISGIFKGHE
ITQAENFRKL LLSMVKDVRV ILVKFADRLH NMRTLEHLNP EKQRRIAQET LEIYAPFAHR
FGLAQFKWEL EDLAFKYLNK VAYDEISNKI SAKRNERESF IKKFAEPISK KLDEYKLKYE
ISGRAKHLYS IYRKMVRRNK PFEEIYDLFA IRIILDTEDK NDCYTTLGIV NQMYPPVADR
FKDYISIPKT NNYQSIHTTI VGPDGKLVEV QIRTRSMHEI AERGFAAHWR YKESKTTSDK
DLENWVNWVR DIFESATKDE EKKDLIENFK LNLYQDEIYV FTPKGDLKRL PLNSTPVDFA
FEIHSKVGHH CIGAKVNGKI VPLDSPLHSG DQVEVIISKN QHPNKNWLKF AVTHKAKNAV
RKYLNKEDEE IVNAGKELWE KKLKKLKLSF NTEDITRLAV SLKFEGTKHF FKSIAQGKLD
LGDVLATTKE KEKKEKVSVL EFDSFASSAR STAGGILVDG KIDGILYSYA KCCNPIPGDP
VIGYVTIGEG VKIHRKSCKN LAMIQEKNEE KFITVQWPEI ETSLFVAGLK IVGKDSPGIL
NDISHAIVSY QNTNIKSVNI STADSAFDGS VTLYVHDISH LERIIERLKK IKGVISVDRF
ENF
//
