ID A0A1W9VJH1_9BACT Unreviewed; 716 AA.
AC A0A1W9VJH1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=(P)ppGpp synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B6226_06155 {ECO:0000313|EMBL:OQY36692.1};
OS Candidatus Cloacimonetes bacterium 4572_65.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1972455 {ECO:0000313|EMBL:OQY36692.1, ECO:0000313|Proteomes:UP000231707};
RN [1] {ECO:0000313|EMBL:OQY36692.1, ECO:0000313|Proteomes:UP000231707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4572_65 {ECO:0000313|EMBL:OQY36692.1};
RX PubMed=28835260; DOI=.1186/s40168-017-0322-2;
RA Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT "Genomic insights into potential interdependencies in microbial hydrocarbon
RT and nutrient cycling in hydrothermal sediments.";
RL Microbiome 5:106-106(2017).
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:OQY36692.1}.
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DR EMBL; NBMD01000142; OQY36692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9VJH1; -.
DR Proteomes; UP000231707; 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; 3.30.460.10; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 49..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 388..449
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 716 AA; 82140 MW; 94C65BF01FBA0E31 CRC64;
MFYKELNSKN FIEELKGLNS KLDIPLIEQA LILAEQLHLN QQRASGEPYL IHPLHVGYIL
GTIKADSQTI CAGLLHDTLE DTSLDYETLS AQFGESIANL VEGVTKLDGF KSSSRKDWIH
HQAENFRKLL LFTVKDVRVI IIKLADRLHN MRTIEYVEQE KKERIAKETL DIYVPLANRF
GLAIIRWELE DICFKILQPD EYHAIVKAID LKRSEREIYI QEVVAPVKSL IEEDSIAVEA
NGRSKHFYSI YRKHLKKSIS YAEIYDLAAI RLITDSSDNC YRILGLLHSL FQPVDDRFKD
YIARPKANQY QSLHTVVIGP EGRKVEFQIR TRAMHKIAEE GVAAHWVYKE SSPVSFNLQI
EAINSILNEQ LDNPSEFLDS LKFNHTYDEI IVITPENDYI KLPVNSSPLD FAFAIHSDIG
LSCSGARVNN KFVPLKTKLK TGDRVEIISS PQSKPSRDWL NLVKTSNARL NIKSYFKKIE
SAEVIFIGKE LFEKRIRKSD FRVKSDEDIL QLAKLFKISS ISEFFASLGK GKISFADVLE
ILTKNNSEND TEEAEIIVEN KPDSQGFHDV IFLDDISNLM LSYAKCCNPK PGDNILGYVT
RGRGITIHKA ECSDPNFLKL LEKESQRFFK ISWNRAKNIV PSMKIDVSGY YNREIHFGIV
ELFNNFNLEI LVNKFSSHGV EFKCHIQFVN NHFKNIKLLI SYLKKLDGVS KVKIIK
//
