ID A0A108UD95_9GAMM Unreviewed; 730 AA.
AC A0A108UD95;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GTP pyrophosphokinase, (P)ppGpp synthetase I {ECO:0000313|EMBL:KWS06814.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:KWS06814.1};
GN ORFNames=AZ78_4372 {ECO:0000313|EMBL:KWS06814.1};
OS Lysobacter capsici AZ78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS06814.1, ECO:0000313|Proteomes:UP000023435};
RN [1] {ECO:0000313|EMBL:KWS06814.1, ECO:0000313|Proteomes:UP000023435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS06814.1,
RC ECO:0000313|Proteomes:UP000023435};
RX PubMed=24762937;
RA Puopolo G., Sonego P., Engelen K., Pertot I.;
RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT to Plant-Pathogenic Oomycetes.";
RL Genome Announc. 2:0-0(2014).
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 GDP: step
CC 1/1. {ECO:0000256|ARBA:ARBA00024329}.
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:KWS06814.1}.
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DR EMBL; JAJA02000001; KWS06814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A108UD95; -.
DR Proteomes; UP000023435; Unassembled WGS sequence.
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; 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; 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; 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;
KW Kinase {ECO:0000313|EMBL:KWS06814.1};
KW Transferase {ECO:0000313|EMBL:KWS06814.1}.
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 657..730
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 554..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 80346 MW; A6C86EDB1F1A1F56 CRC64;
MNVPAAQSRP DLTHVLAQPA AAALAAPLRK ALLEAAQAPQ AGASALDAPA VVAATLDALA
LLDADSDTVA AAILHAYPGW VSAMGAGFER DYPVVAALLD GQRAAGQVWA LHAEQGRHSG
TEGLRRLLLA IVRDLRVVPI LLARQLARMR HADHLPADTR RELAALTRDI HAPLANRLGI
WQLKWELEDL AFRYLEPQTY QKIARLLDEK RGDRERYIEQ VKRTLREAMS AQGLKAEVAG
RPKHIYSIWK KMQRKDAPIS ELYDLRAVRV MVDDVGACYA ALGVVHATWT PVPSEFDDYI
ARPKRNDYRS LHTAVIGPEG KTLEVQIRTH EMHRQAELGV AAHWKYKEAG SHSADAAFDR
KIAWMRRLLD AKGDGGQGGD EALASELDTE LVEDRVYVLT PKGEVIDLPT GATPLDFAYH
VHTEVGHRCR GAKVDGRIVP LDHKLRSGDR VEILTAKTGE PRRDWLVLAN GFLASNRSRE
KVRNWFHKLD RSRNETAGRE LLDKELRRLG LLGADLAPAR ERFTLASDGD LYVQVALGDI
GPHQIGRALL EHERAQSAPP PAATHASGTT VVTPPAPRKL PGKSTDFTVE GVGNLLVQLA
RCCQPLPGEP IVGYLTRGRG VSVHRPGCQA FERLAAATPQ RVLPVEWGRK GSGYEVDIEV
LALDRKWLLK EVTNVIAQSN AHVLSIRSDV ERNGAQVRLR LRLRVADYGQ LSTLLGKLSS
LPAVEYAQRQ
//
