ID A0A1I6ZNJ6_9BACT Unreviewed; 738 AA.
AC A0A1I6ZNJ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SFT64289.1};
GN ORFNames=SAMN04489724_1376 {ECO:0000313|EMBL:SFT64289.1};
OS Algoriphagus locisalis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=305507 {ECO:0000313|EMBL:SFT64289.1, ECO:0000313|Proteomes:UP000199673};
RN [1] {ECO:0000313|EMBL:SFT64289.1, ECO:0000313|Proteomes:UP000199673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23445 {ECO:0000313|EMBL:SFT64289.1,
RC ECO:0000313|Proteomes:UP000199673};
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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; FPBF01000002; SFT64289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ZNJ6; -.
DR STRING; 305507.SAMN04489724_1376; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000199673; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SFT64289.1};
KW Transferase {ECO:0000313|EMBL:SFT64289.1}.
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 738 AA; 84530 MW; 63E11399126051A3 CRC64;
MIEVDIEEER KEILKRYRKL LRQAKPILKP GDAKLIKRAF NVSLEAHKDM RRKSGEPYIY
HPLEVALVCV EEIGLGTTSI VAALLHDVVE DTEWELEDIE REFGYKVMTI IDGLTKIAGV
FESGSSQQAE NFRKMLLTLS DDVRVILIKL ADRLNNMRTL ASMPRHKQLK IASETMYLYA
PLAHRLGLYT IKSELEDLYL KYTDTATYKD IVFKINESKS YRNKFIRSFI LPIEEELKRT
GLDFTIKGRP KSVFSIYNKM KKQGIPFEEV YDLFAIRIIL NSDLESEKAD CWQVYSIVTD
FYRPNPDRLR DWISTPRSNG YESLHTTVMS GTGQWVEVQI RTERMDEIAE RGYAAHWKYK
DRENSKGPSG LDDWITQVRG LLESNDGNAI EFMDDFRGNL FHDEVFVFTP KGDLKVLPFG
STALDFAFEI HTEVGAKCIG AKVNQRLVPI SHKLKNGDQV EILTSNKQKP TEDWLNNVVT
TRAKAKIKDA LREDKKSAIL DGREIVQRKM KQMKMEFNSE SVDKLRAFFE LKTANEFYYR
VGIGAIDPTS IKSFKEFKAT QKLQNKSSQE KVRDESSFTK EIKSLKGPDH DQLLIGEDMD
VVDYILAKCC NPIPGDDVFG FVTVNEGIKI HRTSCPNALE LLSNHGNRVI KARWTSQKEI
AFLAGLRILG TDRVGLINDV TKVISNELKV NMRSITVDSD SGIFEGTIKL YVHSTEHLDK
LIENLVEVDG ILKVSRFD
//
