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
//