ID A0A1H2GQD7_9PSED Unreviewed; 747 AA.
AC A0A1H2GQD7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216580_1906 {ECO:0000313|EMBL:SDU21731.1};
OS Pseudomonas guangdongensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245526 {ECO:0000313|EMBL:SDU21731.1, ECO:0000313|Proteomes:UP000243063};
RN [1] {ECO:0000313|Proteomes:UP000243063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC 2012022 {ECO:0000313|Proteomes:UP000243063};
RA Varghese N., Submissions S.;
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; LT629780; SDU21731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2GQD7; -.
DR STRING; 1245526.SAMN05216580_1906; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000243063; Chromosome i.
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:SDU21731.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243063};
KW Transferase {ECO:0000313|EMBL:SDU21731.1}.
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..747
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 747 AA; 84098 MW; B73A12A56403A55B CRC64;
MVQVRAQQPV NTDGSINLEA WLEHIQGIDP ALDRDSLRQA CEFAREVEAQ AVAAQHIWAE
GMSSFRTGLE IAEILAELKL DQESLLAGVL YRAVREGKTS LEQVEKRFGA TVAKLIEGVL
RMAAISTSLN PRHSMVLGTQ TQVENLRKML VAMIDDVRVA LIKLAERTCA IREVKNAADE
KRYRVAREVF DIYAPLAHRL GIGHIKWELE DLSFRYLEPV QYKQIATLLH ERRLDREQYI
NSVMQQLRDE LSATGIEADI SGRAKHIYSI WRKMQRKGLE FSQIYDVRAV RVLVPEVRDC
YTALGIVHTL WRHIPKEFDD YIANPKENGY RSLHTAVIGP EGKVLEVQIR TESMHEEAEL
GVCAHWLYKG TDVNSGSNHY EEKIAWLRQV LEWHEELGDI GGLAEQLRVD IEPDRVYVFT
PDGHAIDLPS GATPLDFAYR VHTEIGHNCR GAKVNGRIVP LNYSLQTGEQ VEIITGKHGA
PSRDWLNPHL GYVTTSRARA KIVHWFKLQA RDQNVIAGKN YLERELARLA LLAVDFDKLA
EKCNLKSAED MYAALGAGDL RLAQVVNAAQ QLLEPERGFD QIELTPRRQS SVRGSARDEI
QILGVGNLLT QMARCCQPVP GDAIVGYITQ GRGVSIHRQD CPMALQQSER EPERMIQVAW
GHAPAKTYPV DIQIRAYDRS GLLRDVSQIL LNEKINVLAV NTQSDKSANT ANMRLTIEIP
GMAALGRLLA RISQLPNIIE ARRSRAA
//
