ID A0A143XVY0_9FIRM Unreviewed; 773 AA.
AC A0A143XVY0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA_2 {ECO:0000313|EMBL:CVI72084.1};
GN ORFNames=NDGK_02439 {ECO:0000313|EMBL:CVI72084.1};
OS Clostridiales bacterium CHKCI001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1780378 {ECO:0000313|EMBL:CVI72084.1, ECO:0000313|Proteomes:UP000198774};
RN [1] {ECO:0000313|EMBL:CVI72084.1, ECO:0000313|Proteomes:UP000198774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC1 {ECO:0000313|EMBL:CVI72084.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; FCNS01000037; CVI72084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XVY0; -.
DR STRING; 1780378.NDGK_02439; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000198774; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CVI72084.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198774};
KW Transferase {ECO:0000313|EMBL:CVI72084.1}.
FT DOMAIN 75..175
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 419..482
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 699..773
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 773 AA; 88722 MW; 81B99EF581717B7A CRC64;
MTETLEMIQE LNQKDKPKPA VTAPEDFTDP DQLYQILIKT IKKYHPSDDI SMIEKAYHVA
KESHGDQKRK SGEPYIIHPI CVAIILAELE LDKESIIAGL LHDVVEDTAM TNEDMRREFG
EEIALLVDGV TKLTQIKWYK DKVEVQAENL RKMFLAMAKD IRVIMIKLAD RLHNMRTLQY
MKPEKQKEKA RETMEIFAPI AERLGISKIK VELDDLSLMY LEPEVYHDLK KKLELTAPTR
EHFIENIIEE VSTRLKQENI EASLSGRVKH LFSIYKKMVN QNKTLDQIYD VFAIRVIVEN
IRDCYAVLGI IHEMYQPMPN RFKDYIAMPK PNMYRSLHNT LIANNGQPFE IQIRTYEMHR
VAEYGIAAHW KYKERGSGKT TIKAEEKKLS WLRQILEWQK DMDDNKEFLS VLKNDLNLFS
ENIYCFSPKG DLKTLPMGST PIDFAYSIHS AVGNRMIGAK VNGKLVTIDY KLQTGDRVEI
ITSQNTKGPS RDWLNIAKSS QAKSKINQWF KAERKEENIV RGKELVQAYC KAKGIQMTNI
MKPEFMQKAL DKYGFKDWDS MMAAIGHGGL KEGQIVNKMQ EEYTKTIKKT VTDQDILNAV
KENNAKLQAA EKEKGKQKEK QSPVWIEGMG NMPCRFPKCC SPVPGDEIVG YITRGRGVTV
HRTDCTNIIT LPDSEKVRLK EAEWDRSVLQ NVDTKFTVEL QIYCYNRVGM LSHITALFSD
KGINLENVNT TSGKQGTATI TVGFKVTGMQ ELQRITNMLQ ALEGVLDVKR NVG
//
