ID A0A1R4FD76_9ACTO Unreviewed; 727 AA.
AC A0A1R4FD76;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GTP pyrophosphokinaseppGpp synthetase I {ECO:0000313|EMBL:SJM53827.1};
GN ORFNames=CZ771_06600 {ECO:0000313|EMBL:SJM53827.1};
OS Actinomycetales bacterium JB111.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM53827.1, ECO:0000313|Proteomes:UP000196124};
RN [1] {ECO:0000313|EMBL:SJM53827.1, ECO:0000313|Proteomes:UP000196124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB111 {ECO:0000313|EMBL:SJM53827.1,
RC ECO:0000313|Proteomes:UP000196124};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUHX01000032; SJM53827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4FD76; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000196124; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SJM53827.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000196124};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SJM53827.1}.
FT DOMAIN 39..136
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 380..443
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 647..721
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 727 AA; 80792 MW; 415E875FB347D1E8 CRC64;
MIGALRANHP KSDVALVKRA YEVAERAHDG QMRKSGEPYI THPVAVTTIL AELGMPDVVL
AAALLHDTVE DTDYSLDQVR SEFGDEIALM VDGVTKLDKV HYGEAAQAET VRKMVVAMAK
DIRVLVIKLA DRLHNARTWK YVSQESASRK ARETLEIYAP LAHRLGVNTV KWELEDLSFR
TLYPRVYDEI DHLVAERAPA REEYLGQVRK QIEADLKTHR LKAVVTGRPK HHYSIYQKMI
VRGRDFEDIF DLVGVRVLVD TINDCYTMLG AVHARWTPMP GRFKDYIAMP KFNLYQSLHT
TVLGPGGRPV EIQIRTHEMH RRAEYGVAAH WKYKSNAAGR AQAGAEPGAS EMGWLRQLVD
WQRETADPGE FLDSLRYEMA GSQVYVFTPK GDVQALPAGA TPVDFAYAVH TEVGHRTVGA
KVNGKLVPLD RKLDNGETVE IISSKAPESG PSKDWLSFVA SPRAKNKIRQ WFTKERREEA
VEEGKTALAR AMRKQNMPIQ RLMSAEAVHS LAVEMRYQDV EGLYVAIGEG HVSASNVVSK
LVQVMGGDDG AEETLAEATI PGGFTPVKRT GNQGVTVAGM EDTDVWVKIA RCCTPVPGDP
IVGFITRSQG VSVHHAECQN VEQLKQQPER LVEVSWADST SSTFLVQMQV EALDRHGLLS
DLTRVLSDNH VNILSASITT TRERVALSKF VFEMGDTAHL GSVLSAVRRV QGVLDVRRVM
GRKTEAS
//
