ID A0A249KP97_9ACTN Unreviewed; 719 AA.
AC A0A249KP97;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:ASY18611.1};
GN ORFNames=A1sIA105_03500 {ECO:0000313|EMBL:ASY18611.1};
OS Candidatus Planktophila versatilis.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884905 {ECO:0000313|EMBL:ASY18611.1, ECO:0000313|Proteomes:UP000217175};
RN [1] {ECO:0000313|EMBL:ASY18611.1, ECO:0000313|Proteomes:UP000217175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-105 {ECO:0000313|EMBL:ASY18611.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-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; CP016775; ASY18611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KP97; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000217175; Chromosome.
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:ASY18611.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ASY18611.1}.
FT DOMAIN 48..145
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 647..719
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 719 AA; 79758 MW; DD43DF99C8C7D8B3 CRC64;
MDTETLIAPL IGALKEHHPQ SNGAEIERAF KIARTAHEGQ LRKSGEDYIT HPVAVSLILA
ELGLNEITIV ASLLHDTVED TPYSLQQLRT DFGDEIANLV DGVTKLDKLT YGPTAEAETV
RKMVIAMSRD IRVLVIKLAD RLHNARTWGF VSAESAQRKA QETLDIYAPL AHRLGMNAIK
WELEDLSFAV LEPKKFEEIS RLVAERSPSR DALTSEVVDA VEKDLQRDLI TATVTGRNKH
FFSVYQKMVV RGREFNEIYD LVGIRVLVND VKDCYAVLGS IHARWSPVPG RFKDYIAMPK
FNLYQSLHTT VIGPNGKAIE IQIRTYEMHS RAEFGIAAHW KYKQSGEPET NTPEMMWLRQ
LHEWQKETED PSEFLEALRF DLGSPEVFVF TPKGSVVALP GGSTPVDFAF SVHTDVGLRC
AGAKVNGRLV PLESELVNGD VIEIVTNKGE HAGPSRDWLN FVKSPRARSK IKAWFSKERR
EEAIDAGRES IARQMRKAGL PLQKIFAGHA LLELAHDMHY ADIDALYNAV GDGHVSAASI
VEKLTASMSG EDSHPEVTIE NIPTGMQVTK RTSSAVEVEG VDDVLVKLAR CCTPVPGDAI
MGFITKGSGI SVHREDCINA TDLRENQGER VVGVKWLLGA ASLFLVNIQV EALDRARLLA
DVTRTLSEQH VNILSAAVST SKDRVAISRF TFEMADAKHL DSVLAAVRNI EGVYDVYRT
//
