ID A0A1F5Y146_9BACT Unreviewed; 571 AA.
AC A0A1F5Y146;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=GTP pyrophosphokinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3G54_03115 {ECO:0000313|EMBL:OGF93928.1};
OS Candidatus Giovannonibacteria bacterium RIFCSPLOWO2_12_FULL_44_15.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1798364 {ECO:0000313|EMBL:OGF93928.1, ECO:0000313|Proteomes:UP000178894};
RN [1] {ECO:0000313|EMBL:OGF93928.1, ECO:0000313|Proteomes:UP000178894}
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:OGF93928.1}.
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DR EMBL; MFIQ01000001; OGF93928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5Y146; -.
DR STRING; 1798364.A3G54_03115; -.
DR Proteomes; UP000178894; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; PF01842; ACT; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 390..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 497..571
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 571 AA; 65777 MW; FA7F84F782C92593 CRC64;
MTWEEYEKKL SKFNVAEKDK EFLKRAFELA LRVHKDEKRL SGEDFITHPI AVSLKLAKLK
MDANTIAAGL LHDAVECSPE TLKTIKKNFG EELSFLVDGV TKVDRIHATG ADRALESVKK
MFLAVAEDIR VVIIKLMDRL HNMETVGSLP QEKRERIARE TLTLYASIAD RLGMWNIKAQ
LEDLSMKYLY PKEYEYISNE IKKFAPGREK YLKKILRVLE VELKKAEIKP VEINYREKHL
YSAWQKLERY EGDWSRISDL IALRIIVPDI KSCYGALGVV HKLWKPVPGK FKDYIALPKP
NGYQSLHTSV FTEPRVIVEF QIRTLEMHRE AESGIAAHWA YSEAGKPKRG FKSMGKKFNW
ISQLQDWNKE LKKENTSSEE FLEALKIDFF KDRIFVLTPK GDVIDLPKGS TPLDFAYHIH
SEIGNHASGA KINGRMMSFS WELRSGNVVE IITQKNKKPS VEWLTLVRTA LAKSKIRQAL
RIYPKKSFLS SDKKLAEIRI YGKNRIGFIK DITSVFAKRK INIQNLISAR SGSEEVPIRV
TCVPKDKVEL ENIVLRLKKI EGVRKVAFIL K
//
