ID A0A380BTP2_SPOPA Unreviewed; 732 AA.
AC A0A380BTP2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=relA {ECO:0000313|EMBL:SUJ06943.1};
GN ORFNames=NCTC4822_01784 {ECO:0000313|EMBL:SUJ06943.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ06943.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ06943.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGYZ01000002; SUJ06943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380BTP2; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000254519; 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:SUJ06943.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000254519};
KW Transferase {ECO:0000313|EMBL:SUJ06943.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 658..732
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 732 AA; 84039 MW; 417FAFFFCBCFA8FA CRC64;
MAKDKDMTAE DIFTLVSSYM NDEHVDFVKK AYEAAKSAHE GQYRSSGEAY ILHPVQVAGI
LAELQMDPAT VAAGFLHDVV EDTEVGRDDI IEEFGEEVAM LVDGVTKLER LKYRSKEEKQ
AENHRKMFVA MAQDIRVILI KLADRLHNMR TLRHVSVEKQ RRVSAETLEI FAPLAHRLGI
STIKWELEDI ALRYLKPQQY YRIVNMMKQK RVEREDYLED LMDQMKTEIN KMNIEADLSG
RPKHLYSIYR KMVLQEKEFE EIYDLLAVRI IVKSIKDCYA VLGIIHTLWK PMPGRFKDYI
AMAKQNLYQS LHTTVVGPGG DPLEVQIRTE EMHKIAEYGV AAHWAYKEGK SASNNPKDID
SKLTWFREIL EFQNESSDAE EFMESLKFDL FSDMIYVFTP QSDVIELPAG SVPIDFAYRV
HSEVGNRTIG AKVNGKMVPL DTELHTGDII EILTSNNSFG PSRDWLKIAH SSQAKNKIRQ
FFKKQLRQEN IEKGREMIEK EIRDQDFAVK DIYTTSNISR VCDKFNFASE EDMCAAVGFN
GITAEQVVNR LAEKLKRERV EQDKINKIVT DMQTNQPTRV TESGVIVKDI DNLLIRLSKC
CNPVPGDDIV GFITKGRGVS VHRADCPNVQ HTREEDNRLI DVEWAVGRTD DRKEFQVDIE
ISAFDRHGLL NEVMMVVAET KTTMVAVSGK ADKENIAKIN MSIKIKNIAH LHRIVDRIKQ
VRDIYSVERV IN
//
