ID Q8XJ23_CLOPE Unreviewed; 726 AA.
AC Q8XJ23;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA {ECO:0000313|EMBL:BAB81644.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81644.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB81644.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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; BA000016; BAB81644.1; -; Genomic_DNA.
DR RefSeq; WP_011010694.1; NC_003366.1.
DR AlphaFoldDB; Q8XJ23; -.
DR STRING; 195102.gene:10491207; -.
DR KEGG; cpe:CPE1938; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
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:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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; SM00471; HDc; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB81644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB81644.1}.
FT DOMAIN 43..142
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 387..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 652..726
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 552..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 695..725
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 726 AA; 83103 MW; 83977EF0316FD7A1 CRC64;
MLEELISKIK ANGNNVDIDL VKKAYDLAFE AHKEQKRESG EPYITHPISV AMILADMGMD
TNTIVAGLLH DVIEDTDYTY EDISNIFNVE VANLVDGVTK LGKIKYKSKE EQQADNVRKM
LLAMAKDIRV IIIKLADRLH NMRTLKYMKP EKQKKKAQET LDIFAPLAHR LGISKIKWEL
EDLCLRYIHP EEYYDLVNMI AEKRVEREKF ISRIIKELKE NLDKANIDSD IEGRPKHFYS
IYRKMVNKHK SIEQIFDLTA IRILVNTVKD CYAVLGIVHT IYKPIPGRFK DYIAMPKPNM
YQSLHTTVIG SEGKTFEIQI RTFEMHRTAE YGIAAHWKYK SGINGTDSKD MTFENKLTWL
RDILEWQKEA VDATEFMEGF KLDLFSDEIF VFTPKGVVIN LPAGATPIDF AYKIHTDIGN
KCVGAKVNGK IVTLDYKLKT GEIVEILTSS SSRGPNIDWL NIANSNQARS KIKQWLRKAR
REENLERGKE MLDKECKKQS LVFSDLSKGP LYDKLLKRYH LNNVEEIYVA IGEGELLSST
VISKLKENIV KQVAEEELNK NIEEQIAKTE RQIKKKQNYG VTVKGLNNIM VRFARCCNPV
PGDDIAGYIT KGRGVSVHRK DCSNFKAIVE KQREKVVDVS WGTEKGAAYV AELEVKAEDR
MCLLSDVMLV ITDSNLSLLS LNAKSGRNGV ANINIQVKID NIEQLKELMK KIRRLQGILD
VYRVNK
//
