ID Q0RNT9_FRAAA Unreviewed; 762 AA.
AC Q0RNT9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=GTP pyrophosphokinase ( ATP:GTP 3'-pyrophosphotransferase ppGpp synthetase I (P)ppGpp synthetase) {ECO:0000313|EMBL:CAJ60797.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:CAJ60797.1};
GN Name=relA2 {ECO:0000313|EMBL:CAJ60797.1};
GN OrderedLocusNames=FRAAL2148 {ECO:0000313|EMBL:CAJ60797.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ60797.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ60797.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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. {ECO:0000256|ARBA:ARBA00025704}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CT573213; CAJ60797.1; -; Genomic_DNA.
DR RefSeq; WP_011603313.1; NC_008278.1.
DR AlphaFoldDB; Q0RNT9; -.
DR STRING; 326424.FRAAL2148; -.
DR KEGG; fal:FRAAL2148; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_4_0_11; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ60797.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Transferase {ECO:0000313|EMBL:CAJ60797.1}.
FT DOMAIN 107..204
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 440..505
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 673..747
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 81289 MW; C7ABD75882349E02 CRC64;
MDAETVGAGL PAGGGLTPAL SRADSRGDSS DDASRALSAA RQASVRLAHL ARRMATPRMS
QVPPELRDIV EAHRDYHPRA DIGALVHAYG VAERLHAGQM RRSGDPYISH PLAVCEALAE
LGVDTTTLIA ALLHDTVEDT GYTLDSVVEE FGGEVANLVD GVTKLDKMRF GEAAEAETLR
KLIVALAQDY RVLVIKIADR LHNMRTLDFM SPPKQVKISR VTLEILAPLA HRLGVSVIKR
ELEDRAFAVL HPAEHARTAR IVDEFTAAEQ ASGSLAGLVA RLRAGLAGAR IDSEVSVRAS
HLFSIYKRGQ ERARAPQDYT DIVRVLVLVD EVTDCYAALG VIHALWRPVP GRLRDFVATP
KFNMYQSLHT TVVDDTGRSI DIQIRTPAMH RLAETGIVAR PVGPGADGAR LEGLSWLHSL
LDWQEDTIDS DEFLESLSSD LDSDEVLAFT PKGRMIALPP RSSPVDVAYA VHTDIGHRAI
GARVNGRLVP LHTRLRNGDV VEILTSNLPG AGPSEDWLRF VKTSRARVRI RRRLARQRRD
AAAGPGLPEG PEQSGPAAGT DAGARGGPTG DPGGGPGGAA GGTSAAPARQ LARRGVPSLA
AVADDGSGAS MPVRLARCCL PLPGDAVVGF TTHGSAVSLH RRECGNAAEA SADRERVVVT
AWSAPDVQIF PAEIAVEAFD RYGLLADITE VLSETSVSVR AASTTTSEDR VAHARFTIEV
TGPEQLDSVL SAVRRVGGVY DCYRVCQSQA SPTVDPPARA AT
//
