ID A0A0S8IC95_9CHLR Unreviewed; 720 AA.
AC A0A0S8IC95;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=AMJ88_01025 {ECO:0000313|EMBL:KPK95224.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK95224.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK95224.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK95224.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
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:KPK95224.1}.
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DR EMBL; LJUS01000002; KPK95224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IC95; -.
DR PATRIC; fig|1703387.3.peg.1081; -.
DR Proteomes; UP000051685; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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 44..155
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 396..457
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 646..719
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 720 AA; 81732 MW; 47CB685CC52275F7 CRC64;
MKFEGLIELL PEDTSHADLE SLKRAYKVSQ RAHKGQKRAS GEPYIQHCLA VARILAELGA
PVPAIIAGLL HDTVEDSNLT VLDLERDFGE EVASLVDGVT KLTQLPRVSR RQKGEKDART
IKGELAKETL RKTFLAMGDD VRVVVIKLAD RLHNMRTLVH LPPEKRQRIA EETLEIFAPL
ANRLGIWQMK WELEDLAFRF VHPDEYKGIA AHVAERRVDR EQALEEISLR LKLVLAKAGI
AAEVTGRPKH LYSIYRKMKR KDVPFDMVFD VRGVRIIVER EGQCYLALGV IHNEWKPIPG
TFDDYIATPK DNFYQSLHTA VVYDDGGTLE VQIRTPEMHR NADYGIAAHW HYKEGRLSDD
VFEQRILWLR RLMEWRQDID DAADFVDAMK SDVFDDRVYV FTPKGDIIDL PAGSTPIDFA
YHIHTDIGHR CRGAKVNGKL ISLSQKLQTG DSVEILTTKR GGPSRDWLNP SLELAKSQRA
RNKIRQWFRR RNRELNVSHG RLLLDRELRR LGIEGYSYEK ISNELGYTQT DDLLAAIGCG
DVHLSKIVTQ ILEKDEAGLD FIEEVEAIPV AELKADEISI LGVSGLLVHL GRCCNPAPGD
PIVGYITRGR GATIHRQDCP NVLRIKDRER LVQVSWGRPQ QTYPVSVRIQ AYDRDGLMRD
VSTLVSNEGI NMSSIHLSTK NSLAIFDLVM RITDVTQLSR VLNRLEALPN VLEARRLRPG
//
