ID C6YTZ2_9GAMM Unreviewed; 642 AA.
AC C6YTZ2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=BZ13_901 {ECO:0000313|EMBL:AJI75318.1};
OS Francisella philomiragia subsp. philomiragia ATCC 25015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI75318.1, ECO:0000313|Proteomes:UP000031897};
RN [1] {ECO:0000313|EMBL:AJI75318.1, ECO:0000313|Proteomes:UP000031897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O#319L {ECO:0000313|EMBL:AJI75318.1,
RC ECO:0000313|Proteomes:UP000031897};
RX PubMed=25931589;
RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT "Genome sequencing of 18 francisella strains to aid in assay development
RT and testing.";
RL Genome Announc. 3:0-0(2015).
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; CP010019; AJI75318.1; -; Genomic_DNA.
DR RefSeq; WP_004287138.1; NZ_DS999312.1.
DR AlphaFoldDB; C6YTZ2; -.
DR KEGG; fpt:BZ13_901; -.
DR PATRIC; fig|539329.6.peg.888; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR Proteomes; UP000031897; Chromosome.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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;
FT DOMAIN 398..459
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 642 AA; 73713 MW; 1BD0DB5C4706D370 CRC64;
MQVIDSKLLD SDGQIKDDLL ISELKSFYTS DKFEIIAAAL ELLKSKSAES VRHPTGISSF
LYAIEMAYVL FKIKADEESV SAGILYELYN FGDISDEDVE KATNQTVVKI LQGTRKMSAI
RMYRSDNISL EQIDTFRKML LTIIEDVRIV LIKIVDKLCT IRHLKSLNTN TQRVIARETL
DIYAPLANRL GLGAIKWELE DRAFFFLEQE EYKKIAKSLG FTRKEREEFL NQVIEELKQI
LRKYNLDAGV QGRVKHIYSI YKKFKNKGYQ DINDLYDITA VRVITNNIDE CYKVLAEVNN
LYSPIPEEFS DYIANPKPNG YKSIHTVVRV GEQNLEVQIR THKMHEESEL GFAAHWRYKE
GVKFDASYEA RVAWLRSLLE WEKEINDDDS QITKELNRRL YVFTPANELI DLAEDSTVLD
FAYSVHTMVG HRTKGVKLNG KIVPLTTKLK TGDKVEVLTG KEPNPSKDWA SESLGYLTSA
RNRSRVTKWF NEQNKEDNIV LGKDRLLKEL RGYDLKEVDF VEVANKFNMK SSDSLFVAVE
NGTVRINSIV NHILDTYSAE EKLVKKQNRV TTAKTKTPKV LVSGFNGMKY EMAKCCQPVY
PDEIQGYMSV TKGVVIHTSS CPNLGHLKEK SPEKFIEVNW DE
//