ID A0A1I4JDK0_9BACI Unreviewed; 726 AA.
AC A0A1I4JDK0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SAMN04488054_103102 {ECO:0000313|EMBL:SFL64639.1};
OS Salibacterium qingdaonense.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=266892 {ECO:0000313|EMBL:SFL64639.1, ECO:0000313|Proteomes:UP000199668};
RN [1] {ECO:0000313|EMBL:SFL64639.1, ECO:0000313|Proteomes:UP000199668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6134 {ECO:0000313|EMBL:SFL64639.1,
RC ECO:0000313|Proteomes:UP000199668};
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; FOTY01000003; SFL64639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4JDK0; -.
DR STRING; 266892.SAMN04488054_103102; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000199668; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFL64639.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000199668};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFL64639.1}.
FT DOMAIN 44..143
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 386..447
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 652..726
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 549..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 83505 MW; F3608BF8BFC81A8E CRC64;
MTIDEVLEKS REFLTEDDVS FLQRAYKYAE EAHKDQYRKS GEPYILHPIQ VVGILVELQM
DPDTLAGAFL HDVVEDTEVT VEDIEEAFNE EVAMLVDGVT KLKKIKYKSK EEQQAENHRK
MVVAMAKDIR VILIKLADRL HNMRTLKHLP PDKQRRISNE TLEIFAPLAH RLGISTIKWE
LEDTALRYLD PQQYYRIVNL MKQKRAEREQ YLDEVINEIK KNMNQTNLEA SELYGRPKHI
YSIYRKMVKQ KKQFNEIYDL LAVRIIVKSI KDCYAVLGII HTCWKPMPGR FKDYIAMPKA
NMYQSLHTTV IGPKGEPLEV QIRSEDMHSV AEFGVAAHWA YKEGKTASGT SLEDKLTWFR
EIIEWQNETA DAQDFMESLK MDLFSDMVFV FSPKGDVIEL PRGSVPIDFA YRIHTEIGNR
TIGAKVNGKM VPLDYQLNTG DIVEMLTSKH SYGPSQDWLK LTQSSHAKNK IKQFYKKERR
EENVSKGRDM VEKELKTQGF DTKQVMTEET KQDTAEKFSF SSEEDMFAAV GYNGVSPKQV
VTRLTDKIRQ QQEEEEEQKP VAEAVKEVTT QTESQNTGAG VKVKGMDNLL IRLSKCCNPV
PGDEIIGFIT KGRGVSVHRK DCPNVKNVEE TSRLLEVEWE AANDKRKNYS VDLEITGYDR
RGLLNEVLQA VTETKTNITA VNGRSDKNKV AVIDVTISIA NIDHLHRVVE KVKKLSDIYS
VRRRVQ
//
