ID A0A1Y0H3Q8_9BACT Unreviewed; 738 AA.
AC A0A1Y0H3Q8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=(P)ppGpp synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CCB81_00340 {ECO:0000313|EMBL:ARU42679.1};
OS Armatimonadetes bacterium Uphvl-Ar2.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004468 {ECO:0000313|EMBL:ARU42679.1, ECO:0000313|Proteomes:UP000195582};
RN [1] {ECO:0000313|EMBL:ARU42679.1, ECO:0000313|Proteomes:UP000195582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar2 {ECO:0000313|EMBL:ARU42679.1,
RC ECO:0000313|Proteomes:UP000195582};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP021424; ARU42679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0H3Q8; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000195582; Chromosome.
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; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000195582}.
FT DOMAIN 57..165
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 405..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 661..733
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 83062 MW; 34652A28CA07CB80 CRC64;
MEAPSAYNDA RVVAAREKLA SKFRELRPDH EDTRIMAAMD LAATAHDGQF RRSGEPYVTH
PVEVALICLE LRLDNDGIIA ALLHDVIEDT EVTNAEVRAQ FGEDVVQLVE GVTKLEKGVR
LDGTANQAAR AETLRAAESL RKMLIAMSLD IRVMIIKLAD RLHNMRTLDS MPSDRRIRIA
QETMDVYAPL AARLGIWQIK WQLEDLSFKV LHPKEFREIT EAVAKSRQHR EDELKESIRI
LKERLESKGL HNTQVIGRPK HLYSIFNKVV KQGIPFEQIY DLIALRVIVS QPYECYLALG
YVHDLWLPMQ GLFSDYISAP KPNGYQSLHT KVIGPHGEPI EVQIRTREMH EIAEYGVAAH
FAYKEGERAN VRGEAIAELR KQIADWSNDS SNSREFLKAV STDFFSEQVF VFTPKGDVLD
LPAGSTPIDF AFRVHTDLGL ITVGAKINGR IVPLSTKLQN GDRVELVTRR DAQPSLDWLE
FVQSQHARSK IRAYFRRRNR AENTSRGKEA IEAELKRLGL EPRALTADDS VQKVLVHFKQ
VDNVADLFAR VGEGLVSVQS VAMRLRELVR PEVPAEAKDP FRLKGSRATQ EARTSMEGVL
SRRARCCLPV PGDDVVAYVS RGRGLLIHRR VCPDAMALMD KEPERMTGLD WEPDDNVYDV
VLIVVTLNRP GLLGEISSLL GELKTNISAV KAKTGPTAEI SLQIDVRDSK HLQHVMNQIG
QMSDVISILR AFGRGKFK
//
