ID A0A0Q7ANL2_9BURK Unreviewed; 745 AA.
AC A0A0Q7ANL2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KQW36375.1};
GN ORFNames=ASC76_16935 {ECO:0000313|EMBL:KQW36375.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW36375.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW36375.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36375.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW36375.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36375.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQW36375.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMDS01000005; KQW36375.1; -; Genomic_DNA.
DR RefSeq; WP_056468923.1; NZ_LMDS01000005.1.
DR AlphaFoldDB; A0A0Q7ANL2; -.
DR STRING; 1736528.ASC76_16935; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051611; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase 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; 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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KQW36375.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611};
KW Transferase {ECO:0000313|EMBL:KQW36375.1}.
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 670..745
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 745 AA; 81661 MW; F244EADAE586835C CRC64;
MKTGVLDARS DAAPIVHLID DHPDAAAEAA QLVRARAFAE PLLYGRLLDT GEDALAHADA
VAAILQGIGA APAMRAAAYL VYAGDYLTKP DEVIAKAFGP SHASLVVNTR KLVQLQRAAR
EAQLGTEARA QQTERVRKML LAFSRDLRVV LLRLASRLQT LRFFAATKTP CTPALAAESL
QVFAPLANRL GIWQIKWELE DLSFRVLEPE RYQQVARLLD ERRVEREQRV ERFRLRLADD
LRAHGLPAEV QGRPKHLYSI WKKMQGKGLD FTQVLDVRAV RVIVPDVPRC YAVLGRVHEL
FRPVTGEFDD YIERPKPNGY QSLHTVVLDD DGRAVEVQIR TQAMHEHAEH GVAAHWAYKD
AGAKGYAGVV ADADQQARIA EARKAVLRQL LAWERDTAAP EHPAGSVAGG AAEDRIYVFT
PAAAVVELPA GATPVDFAYT LHTDLGHRCR GARVDGAMVP LNTALRSGQT VDVIVAKEGG
PSLDWLNAEL GYLKSHRARA KVRAWFNLQA QKETIARGRE SVEKLLQREG KTAIKLDDLA
AQLGFRNADA LFEVVGKDEY SLRNIETLLR PVEALPTPDD LIALRRPSTT APKSGVLVVG
VESLMTSLAR CCRPAPPDAI GGYVTRGKGV AVHRASCTNF RQMAAHSPER VIAVQWGAPR
GDKAALYPVD VMVEAADRQG LLRDITELFA KEKMNVTGVK TQSVKDSGGG TAWMTFTIEV
ADAARLTHVL GLVQHIAGVR SVRRK
//
