ID A0A1L4BVC9_9GAMM Unreviewed; 643 AA.
AC A0A1L4BVC9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=F7310_08565 {ECO:0000313|EMBL:API87802.1};
OS Francisella uliginis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=573570 {ECO:0000313|EMBL:API87802.1, ECO:0000313|Proteomes:UP000184222};
RN [1] {ECO:0000313|EMBL:API87802.1, ECO:0000313|Proteomes:UP000184222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX077310 {ECO:0000313|EMBL:API87802.1,
RC ECO:0000313|Proteomes:UP000184222};
RX PubMed=27881415;
RA Challacombe J.F., Petersen J.M., Gallegos-Graves V., Hodge D., Pillai S.,
RA Kuske C.R.;
RT "Whole genome relationships among Francisella bacteria of diverse origin
RT define new species and provide specific regions for detection.";
RL Appl. Environ. Microbiol. 0:0-0(2016).
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; CP016796; API87802.1; -; Genomic_DNA.
DR RefSeq; WP_072713566.1; NZ_CP016796.1.
DR AlphaFoldDB; A0A1L4BVC9; -.
DR STRING; 573570.F7310_08565; -.
DR KEGG; frx:F7310_08565; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000184222; Chromosome.
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; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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:SF40; GTP PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:API87802.1};
KW Transferase {ECO:0000313|EMBL:API87802.1}.
FT DOMAIN 398..459
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 643 AA; 73706 MW; C0297FA668E53F4F CRC64;
MQVIDSKLLD SDGRIRDELL ISELKSFYSD DKFGIIAAAL ELLKVKNAES IRHPTGINSF
LYAIEMAYVL FKIKADEESV SAGILYELYN FGDISDEEVE QTTNATVVKI LQGARKMSAI
RMYRSDNISL EQIDTFRKML LTIIEDVRIV LVKIVDKLCT IRHLKSLNAK TQRVIARETL
DIYAPLANRL GLGAIKWELE DRAFFFLQQD QYKEIAKKLG LTRKQRESFL NDVIAQLKLA
LKKYGLNDAI QGRVKHIYSI YKKLKKKNYK SLDELYDITA VRVVTDSVDE CYKVLAEVNN
LFSPIPEEFS DYIANPKPNG YKSIHTVVHY QDQNVEVQIR THKMHEESEL GFAAHWRYKE
GVKFDASYEA RVAWLRSLLE WEREINDDDS DITKELNKRL YIFTPANELI DLAEGSTVLD
FAYSVHTMVG HRTKGAKLNG KIVPLTTKLS TGDKVEILTQ KEPNPSKDWA SEGLGYLSSA
RNRSRVIKWF NEQNKEDNIA LGKDRLTKEL RGYDLKEIDF IEVASKFNMK SSDSLFAAIE
NGTVRINSIV NHIIDIYSAE EKLIKKQSRA TVGKPKALKI LVSGFDGMKY ELAKCCQPVY
PDQIQGYMSV SKGVVIHTSN CPNLRHLREK NPEKFIHVEW EKD
//
