ID A0A1G8VXA4_9PSED Unreviewed; 747 AA.
AC A0A1G8VXA4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05216186_102394 {ECO:0000313|EMBL:SDJ70728.1};
OS Pseudomonas indica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=137658 {ECO:0000313|EMBL:SDJ70728.1, ECO:0000313|Proteomes:UP000198706};
RN [1] {ECO:0000313|EMBL:SDJ70728.1, ECO:0000313|Proteomes:UP000198706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21544 {ECO:0000313|EMBL:SDJ70728.1,
RC ECO:0000313|Proteomes:UP000198706};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNFD01000002; SDJ70728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8VXA4; -.
DR STRING; 137658.SAMN05216186_102394; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000198706; Unassembled WGS sequence.
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; 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: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; PF19296; RelA_AH_RIS; 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:SDJ70728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198706};
KW Transferase {ECO:0000313|EMBL:SDJ70728.1}.
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 747 AA; 83757 MW; 905A41B743CD1F32 CRC64;
MVQVRAHQPI NTDGSINLES WLDHVLSLDP ALEREALKDA CEFAREAEQQ ANAAQNLWVE
GTSSFQTGLE IAEILADLKL DQDSLVAAVI YRGVREGKIT LAAVHQRFGP VVAKLIEGVL
RMAAISASLN PRQSMVLGAQ AQVENLRKML VAMVDDVRVA LIKLAERTCA IRAVKHASEE
KRHRVAREVF DIYAPLAHRL GIGHIKWELE DLSFRYLEPE QYKQIAKLLH ERRLDREQYI
TNVVQQLRDE LDATGIKADI SGRAKHIYSI WRKMQRKGLE FSQIYDVRAV RVLVPEVRDC
YTALGIVHTL WRHIPKEFDD YIANPKENGY RSLHTAVIGP DGKVLEVQIR THSMHEEAEL
GVCAHWRYKG TDVKSGSSHY EEKISWLRQV LEWHEELGDI GGLAEQLRVD IEPDRVYVFT
PDGHAIDLPK GATPLDFAYR VHTEIGHNCR GAKVNGRIVP LNYSLQTGEQ VEIITSKQGS
PSRDWLNSNL GYITTSRARA KIVHWFKLQA RDQNVAAGKA LLERELNRVG LPPVDFDRLA
EKANLKTAED LFAALGAGDL RLAHLVNMAQ QLVEPERGNE QLELIPRKHG PHKPGKRGDI
QIQGVGNLLT QMAGCCQPLP GDPIVGYITQ GRGVTIHRQD CATALQLAGR EPERIIQVSW
GPVPVQTYPV DIVIRAYDRS GLLRDVSQVL LNERINVLAV NTRSNKEDST ALMSLTIEIP
GLDSLGRLLA KISQLPNIIE AKRNRAS
//
