ID F3LDE2_9GAMM Unreviewed; 748 AA.
AC F3LDE2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=IMCC1989_1835 {ECO:0000313|EMBL:EGG95098.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG95098.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG95098.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG95098.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(2011).
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}.
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:EGG95098.1}.
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DR EMBL; AEVK01000035; EGG95098.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LDE2; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000010300; 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:EGG95098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010300};
KW Transferase {ECO:0000313|EMBL:EGG95098.1}.
FT DOMAIN 420..481
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..748
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 748 AA; 84406 MW; D3761E86ED1C2505 CRC64;
MVKVREDYPL RDNGDVDIEE WAARIASVAG SDDFAQKQLI SAANLSWHAE RDIAALNKLW
SQHASSFLTG LEMAEILAEL QLDQEALIAA VLYRGVREGK INILDVKERY GDTVERLIYG
VSGMAAISQL RNDSEESALG QRSADQTETV RKMLVSMVDD VRVALIKLAE RTCAIRAVKD
ATDERKQKVA REVFDIYAPL AHRLGIGHIK WELEDLGFRY LKPDDYKSIA KLLDEKRLDR
QDYIDYVVDS LQTQIQKNNI DAEVYGRAKH IYSIWRKMQR KNIGFSEVYD IRAVRILVPT
TKDCYEVLGI VHTLWRNIPH EFDDYIAAPK ENGYRSLHTA VVGPSQRVIE VQIRSHSMHE
EAEYGVCSHW RYKGTDSSDT DTQVDSYEQK IEWLRQVLDW HEELGVEGLT DDIGSSVEQD
RVYLFTPEGH VIDLPLGATP LDFAYRVHTE IGHRCRGAKV SGKIVPLNHV LKTGDQVEIL
TGKQTVPSRD WLMDGLGYLH TSRAKAKVRQ WFGEQAREQN IADGRAILDK ELRRLGVRDI
NFEDLLKVLK HKELDDLYAH VGSGEITLSQ VLRASQKLLE PSVPEQTEIN FSNKTPTTAG
TDVYIDGVGN LLTNIAHCCN PLPGDDINGY ITLGKGVSIH RKDCRNILQL AADEPARIIQ
VDWGEAPTQT YAVDVLIDAY DRIGLLSDVT TVLDSARINV SAMQTLSDRG ENTVSMVVTI
DIRDFAHLSH ILARLNQLPN VATARRKN
//
