ID F9PGI5_9ACTO Unreviewed; 774 AA.
AC F9PGI5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=GTP diphosphokinase {ECO:0000313|EMBL:EGV14547.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:EGV14547.1};
GN Name=relA {ECO:0000313|EMBL:EGV14547.1};
GN ORFNames=HMPREF9058_2472 {ECO:0000313|EMBL:EGV14547.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14547.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV14547.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14547.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV14547.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFUR01000001; EGV14547.1; -; Genomic_DNA.
DR RefSeq; WP_009747358.1; NZ_AFUR01000001.1.
DR AlphaFoldDB; F9PGI5; -.
DR GeneID; 64212572; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000004281; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; GTP PYROPHOSPHOKINASE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGV14547.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:EGV14547.1}.
FT DOMAIN 80..177
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 428..489
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 695..769
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 774 AA; 85883 MW; EF628D347B9EDF9D CRC64;
MTETKNTPDT SGDSVVPGSR VRSRLAWFGS RGHSTPAAIE PLLRAVRANH PKADTSLIVR
AYEVAEKAHS GQRRKSGEPY ITHPVAVATI LAELGMTAQT LAAAVLHDTV EDTDYTLERL
RADFGDEISL LVDGVTKLDK LQYGEAAQAE TVRKMIIAMS KDIRVLVIKL GDRLHNARTW
KYVSAENAAR KAKETLEIYA PLAHRLGMNT IKWELEDRSF KALYPGVYEE IEHMVAERAP
AREEYLRQVR LQIEEDLRVN KIKGAVTGRP KHYYSIYQKM IVRGKDFDDI YDLVALRVIV
DTVQDCYAVL GSLHSRWTPM SGRFKDYIAV PKFNLYQSLH TTVVGPGGKP VEIQIRTHEM
HRMAEYGVAA HWRYKEDPNA SGPSALGGRP GDSDQGDMGW LRQLVDWQKE TQDPTEFLDA
LRYEMAGDQV YVFTPRGDVL ALPAGATPVD FAYAVHTEVG HRTVGARVNS RLVPLDTRLE
NGDTVEVFTS KAINAGPSRD WLSFVASTRA RNKIRSWFSK ERREEAIEEG KGAIARTLRK
QNLPLQRLMS HETLMNVAKT LDKVDIDGLY AAVGEGHVSA QHVVDTLVAT MGGEDGAEET
LAEGILPTRA TTHRRPRTAD AGVVVAGMDE GDVYVKLARC CTPMPGDPIV GFITRGSGVS
VHRADCQNVE QLQREPERLI TVSWADHAQS AYLVQVEVEA LDRGGLLADI TRALADSHVN
LVSASIATSR DRVVTGRFVV ELAEVGHLDH TLAALRRIDG VFEARRSLST TRRR
//