ID A0A1G8PM95_9BACI Unreviewed; 733 AA.
AC A0A1G8PM95;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=SAMN04490247_0067 {ECO:0000313|EMBL:SDI93325.1};
OS Salimicrobium halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=86666 {ECO:0000313|EMBL:SDI93325.1, ECO:0000313|Proteomes:UP000199225};
RN [1] {ECO:0000313|EMBL:SDI93325.1, ECO:0000313|Proteomes:UP000199225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4771 {ECO:0000313|EMBL:SDI93325.1,
RC ECO:0000313|Proteomes:UP000199225};
RA de Groot N.N.;
RL Submitted (OCT-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; FNEV01000001; SDI93325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PM95; -.
DR STRING; 86666.SAMN04490247_0067; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000199225; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP 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; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDI93325.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDI93325.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 392..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 659..733
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 547..574
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 733 AA; 84398 MW; A0A6681237B92AC9 CRC64;
MAKDNVLTAE EVIDGARHYL NGDDLDFIRK AYEYAAWAHR DQYRKSGEPY IIHPVQVAGI
LVNLELDPET IASGFLHDTV EDTDVTVEDL KKAFNEEVAM LVDGVTKLGK IKYKSKEEQQ
AENHRKMFVA MAKDIRVILI KLADRLHNMR TLKHLPAEKQ RRISNETLEI FAPLAHRLGI
STIKWELEDT ALRYLNPQQY YRIVHLMKQK RNEREHYVDE VINEIRSELD QVNIGADLHG
RPKHLYSIYK KMVLQNKQFN EIYDLLAVRI LVNSIKDCYA VLGIIHTCWK PMPGRFKDYI
AMPKPNLYQS LHTTVIGPKG DPLEVQIRTH EMHEIAEYGI AAHWAYKEGK QASGTQTFEE
KLSWFREIME WQSETHDAEE FMESLKMDLF SDMVYVFTPK GDVIELPSGS NPLDFAYRIH
TEIGNQTIGA KVNGKMEPLD YVMKTGDIVE VMTSKHSYGP SEDWVNIAQT SQAKNKIKQF
FKKQRKDENV SKGREAVDRE IKNLDLSPKE VLTPDNIQRV LDKFNFSSVE DMYAAVGYQG
ITAIQVANRL TEKIRRQKEK QEALEDTVAN VNKKDVKKQP NVKKDSGVVV EGIDNLLVRL
AKCCSPVPGD DIIGYITKGR GVSVHRTDCP NVNTEEAQDR LLPVKWETDE QNSKQYHVDL
EIWGYDRRGL LNEVLQAVNE TKTNITAVSG KSDRNKMATI HITILIQNTD HLRKIVDRIK
QIQEVYTVRR VMQ
//
