ID A0A292RHL5_9BACT Unreviewed; 738 AA.
AC A0A292RHL5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:DAA97898.1};
GN ORFNames=CPT80_00890 {ECO:0000313|EMBL:DAA97898.1};
OS Candidatus Gastranaerophilales bacterium HUM_9.
OC Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA97898.1, ECO:0000313|Proteomes:UP000218540};
RN [1] {ECO:0000313|EMBL:DAA97898.1, ECO:0000313|Proteomes:UP000218540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUM_9 {ECO:0000313|EMBL:DAA97898.1};
RX PubMed=28360330; DOI=.1126/science.aal3794;
RA Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT "On the origins of oxygenic photosynthesis and aerobic respiration in
RT Cyanobacteria.";
RL Science 355:1436-1440(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:DAA97898.1}.
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DR EMBL; DABG01000003; DAA97898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292RHL5; -.
DR STRING; 1916320.GCA_002103075_00706; -.
DR Proteomes; UP000218540; 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 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 388..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 637..711
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 738 AA; 84517 MW; A27EADD832046B06 CRC64;
MESQLSLYDD IREKLIEQHR SEEDLALIEK AFLFAQRLHQ NQYRVSEEPY IIHPVEVVKI
LIDLRADTHT LIAGFLHDIL EDTDTTPEEI RELFGDDVLG LVQAVTKLGK LKFKSKEERQ
AENFRRLFIA MANDARVIFL KLADRLHNMR TLNYMAPAKQ QRIAQETLDI FAPLANRLGV
GKIKAELEDL SLKYLHPDKY YEIAKLVSQK KAERESTVQL LIEHISKDVK KNGINAQITG
RAKHYYSIYN KMRRQNVAFH DLYDITAVRV IVDTEKECYE VLGLIHSQFK PIPGRFKDYI
AMPKGNMYQS LHTSVIGPNK KPLEVQIRTW QMHEIAEYGV AAHWRYKEKG SQKADSASDV
QFSWMRKLVE YNNDSSDAED YVNSVKLDLF SDQVFAFTPN GDVLDLPKDA TPLDFAYRIH
SDVGHKTVGA LINGRIAQLD SKLKNGDIVE ILTSKVSAPK LGWLNFVVTK QASSKIRQWF
KKNKREDHIE LGKSTIEHEL TKAVFDEYMK NGEMERVAKL MNYVSVDDLF AALGYGETTI
NKIVNKLKPQ EKSQEPKLKH EHKYSKKKDI VGLEGMLYSF ARCCSPIPGE PIVGVVTRSK
GVTIHRLDCK TLNDIEPERL LDIKWSEVST DRKYTTSIRI ETAEKQGLLK DIITAVSDNN
TNIVFANVKS RNNKLGIIEL GIELDNITTL KAVMNSLQAM PEVYSVKRVQ TAFNQAPKQF
AKKNTKYARK SKTSQNPR
//
