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Database: UniProt
Entry: A0A1K2II24_9FLAO
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Original site: A0A1K2II24_9FLAO 
ID   A0A1K2II24_9FLAO        Unreviewed;       741 AA.
AC   A0A1K2II24;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SFZ92084.1};
GN   ORFNames=SAMN05428642_102521 {ECO:0000313|EMBL:SFZ92084.1};
OS   Flaviramulus basaltis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flaviramulus.
OX   NCBI_TaxID=369401 {ECO:0000313|EMBL:SFZ92084.1, ECO:0000313|Proteomes:UP000182544};
RN   [1] {ECO:0000313|EMBL:SFZ92084.1, ECO:0000313|Proteomes:UP000182544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18180 {ECO:0000313|EMBL:SFZ92084.1,
RC   ECO:0000313|Proteomes:UP000182544};
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; FPKV01000002; SFZ92084.1; -; Genomic_DNA.
DR   RefSeq; WP_072401478.1; NZ_FPKV01000002.1.
DR   AlphaFoldDB; A0A1K2II24; -.
DR   STRING; 369401.SAMN05428642_102521; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000182544; 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; 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:SFZ92084.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182544};
KW   Transferase {ECO:0000313|EMBL:SFZ92084.1}.
FT   DOMAIN          407..468
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   741 AA;  84583 MW;  F8F14F0A28B0FD0E CRC64;
     MTEEAIEKEN AAITKAYKEL LKVSYTTLTD DDKKLIRRAF EVALDGHKNQ RRKSGEAYIF
     HPIAVAKIVA QEIGLDATSI ASALLHDVVE DSPDYEIEDI EKEFGKTVAT IVDGLTKISS
     LSKEKDMDVS LQAENFRKML LTLNDDVRVI IIKIADRLHN MQTMDSMRAD KQIKIASETL
     YIYAPLAHRI GLYNIKTELE DLGLKYTEPD VYNDILSKIK ESKEEQDLYI SQFSEVIQNS
     LDKENLDYTI KGRPKSIFSI RRKMLNQGVP FDEVYDKFAI RIIYQCDADP KTEKFLAWKI
     YSIVTDHFRP NPIRLRDWIS SPKGTGYEAL HITVMGPKGR WVEVQIRSNR MNEIAEKGYA
     AHYKYKEGSE KEDNLESWIN RLQEALENPE TNAVDFVEQF KLNLYSKEIF VFTPTGELKS
     LPKGATALDF AFNVHTEVGM KTRGAKVNGK LVTLSHKLKS GDQVDILTSE NAKPNANWLD
     YATTARSRSK IKSALKEDKK RVGEDGKEIL RRKLKQLKIN LDEESINEMV RFFKLKTSLD
     LFYRIGVGSI DNTMLKSYAS SRSNAFMSYI KSKISRKAPI KKEELEKDEV TVKFDSLVFG
     KEEEKLDYKL SNCCNPIPGD NVFGFLTVNE GLKVHKYNCP NAVSLQSNYA YRIMIAKWID
     STQQEFLVKI LITGIDHIGL VNDITTIISE NMHVNMKSIS FQSNDGLFSG KINVVVKNNT
     IIKKLLEKLK KINGIDKVTR V
//
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