ID B1V035_CLOPF Unreviewed; 726 AA.
AC B1V035;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:EDT72788.1};
GN ORFNames=CJD_2520 {ECO:0000313|EMBL:EDT72788.1};
OS Clostridium perfringens D str. JGS1721.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT72788.1, ECO:0000313|Proteomes:UP000003188};
RN [1] {ECO:0000313|EMBL:EDT72788.1, ECO:0000313|Proteomes:UP000003188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA Paulsen I., Sebastian Y.;
RL Submitted (MAR-2008) 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 -!- 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}.
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:EDT72788.1}.
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DR EMBL; ABOO01000005; EDT72788.1; -; Genomic_DNA.
DR RefSeq; WP_003473695.1; NZ_ABOO01000005.1.
DR AlphaFoldDB; B1V035; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000003188; Unassembled WGS sequence.
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:EDT72788.1};
KW Transferase {ECO:0000313|EMBL:EDT72788.1}.
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 695..725
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 726 AA; 83070 MW; 4A910F08343B6803 CRC64;
MLEELISKIK ANGNNVDIDL VKKAYDLAFE AHKEQKRESG EPYIIHPISV AMILADMGMD
TNTIVAGLLH DVIEDTDYTY EDISNIFNVE VANLVDGVTK LGKIKYKSKE EQQADNVRKM
LLAMAKDIRV IIIKLADRLH NMRTLKYMKP EKQKKKAQET LDIFAPLAHR LGISKIKWEL
EDLCLRYIHP EEYYDLVNMI AEKRVEREKF ISRIIEELKE NLDKANIDSD IEGRPKHFYS
IYRKMVNKHK SIEQIFDLTA IRILVNTVKD CYAVLGIVHT IYKPIPGRFK DYIAMPKPNM
YQSLHTTVIG SEGKTFEIQI RTFEMHRTAE YGIAAHWKYK SGVTGTDSKD MTFENKLTWL
RDILEWQKEA VDATEFMEGF KLDLFSDEIF VFTPKGVVIN LPAGATPIDF AYKIHTDIGN
KCVGAKVNGK IVTLDYKLKT GEIVEILTSS SSRGPNIDWL NIANSNQARS KIKQWLRKAR
REENLERGKE MLEKECKKQS LVFSDLCKGP LYDKLLKRYH LNNVEEIYVA VGEGELLSST
VISKLKENVV KQVSEEELNK NIEEQIAKTE RQTKKKQSYG VTVKGLNNIM VRFARCCNPV
PGDDIAGYIT KGRGVSVHRK DCSNFKAIVE KQREKVVDVS WGTEKGTAYV AELEVKAEDR
MCLLSDVMLV ITDSNLSLLS LNAKSGKNGV ANINIQVKID NIEQLKELMK KIRRLQGILD
VYRVNK
//
