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Database: UniProt
Entry: F9PGI5_9ACTO
LinkDB: F9PGI5_9ACTO
Original site: F9PGI5_9ACTO 
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}.
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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
//
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