ID A0A2G3JCJ5_9NEIS Unreviewed; 733 AA.
AC A0A2G3JCJ5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PHV01762.1};
GN ORFNames=CSQ88_10535 {ECO:0000313|EMBL:PHV01762.1};
OS Iodobacter sp. BJB302.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Iodobacter.
OX NCBI_TaxID=1506510 {ECO:0000313|EMBL:PHV01762.1, ECO:0000313|Proteomes:UP000224670};
RN [1] {ECO:0000313|EMBL:PHV01762.1, ECO:0000313|Proteomes:UP000224670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJB302 {ECO:0000313|EMBL:PHV01762.1,
RC ECO:0000313|Proteomes:UP000224670};
RA Jude B.A., Perron G.P., O'Brien K., Doing G., Bettina A.M.;
RT "Draft genomes of phenotypically distinct violacein producing isolates
RT cultured from the Hudson Valley Watershed.";
RL Submitted (OCT-2017) 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:PHV01762.1}.
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DR EMBL; PDZG01000027; PHV01762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3JCJ5; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000224670; 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; 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; 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; 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:PHV01762.1};
KW Transferase {ECO:0000313|EMBL:PHV01762.1}.
FT DOMAIN 408..469
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 662..733
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 733 AA; 82837 MW; E6EBE70097A69753 CRC64;
MVAVTRPLAQ SIAEAADPDR WLSALTERYP PTDIVRLRQA LDWVFEQYGQ RIHTDTGSSL
FQHAVASASI VADLRLDANS VIATLLFALP TQLNQPMELI NTHFGPDVTR LLDGASKVSQ
LRSLAHPAGG KAADAAQQIE AVRKMLIAMV EDIRAVLIKL AWRTQTMHEL AQAPDDVRRR
IAQETLDLFA PLANRLGVWQ IKWELEDLGF RYLHPDTYKK IAKLLDERRV DREKFIDEVL
STLRIELNNA GVKADLMGRP KHIFSIWKKM QKKKLDFSEL YDIRAVRILV PDLKDCYTAL
GIVHNLWQPI PGEFDDYIAH PKGNFYRSLH TAVIGENDKA VEVQIRTIEM HEHAEYGVAA
HWRYKEGGQG DARYEEKIAW LRQLLDWRED MASETQFAET FKAELFDDTI YILTPAGRVI
TLPKGSTPVD FAYHVHTDLG HRCRGAKVNG QIVPLYTALE NGQRVEILSA KEGGPSLDWL
HQGYVKSHRA ASKIRHWIRQ QHQDIAIEAG RSIYDKEAAR CAARDANQDN IAVKLGCKHI
EELFAALGQG EISQRELNQA FRESLAPIEP ISEQPNDFIK AARANGNGEG ILIEGVDKLM
TLLAKCCKPV PPDHVMGFVT KGRGISIHRS DCSTLKRLAS AAPERLINAD WGIQRGHVFA
TDLLVEAHNR GTLLRDLSDI MARERINVTA VNTQNKDQRV LMRFTLEIRD AEQLQRILIK
LQDVNEVIRV IRG
//
