ID A0A3E0H367_9GAMM Unreviewed; 757 AA.
AC A0A3E0H367;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=DFR26_1381 {ECO:0000313|EMBL:REH37605.1};
OS Paraperlucidibaca baekdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Paraperlucidibaca.
OX NCBI_TaxID=748120 {ECO:0000313|EMBL:REH37605.1, ECO:0000313|Proteomes:UP000256774};
RN [1] {ECO:0000313|EMBL:REH37605.1, ECO:0000313|Proteomes:UP000256774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26022 {ECO:0000313|EMBL:REH37605.1,
RC ECO:0000313|Proteomes:UP000256774};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) 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 -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
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:REH37605.1}.
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DR EMBL; QUNR01000003; REH37605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0H367; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000256774; 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:SF40; GTP PYROPHOSPHOKINASE; 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:REH37605.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256774};
KW Transferase {ECO:0000313|EMBL:REH37605.1}.
FT DOMAIN 417..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 675..750
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 757 AA; 85281 MW; 618E1D009C545D36 CRC64;
MVKVRADYPT HGDGSVDFET WLDRVEDYVE LHDRAELLRA CHRAEQLDRE AVARHNVWSA
RTSSFLTGLA MADILAELNL DQESLMAAIL YRGVREGKIE LVQVGKEFGP DIADLIDGVM
RMAAISRLIN PDPRHNNSEA QQLDNVRKML IAMIDDVRVP LIKLAERTFA IRELKDASDE
RKRRVAREIF DIYAPLAHRL GIGHVKWELE DLSFRYLEPE AYKQIAQLLD EKRLDRDGYI
AQVISTVREH LERMGMGPIE VSGRAKHIYS IWRKMQRKGL GFHELFDVRA IRILLPDVRD
CYAALGVVHS LWKHIPREFD DYIATPKENG YRSLHTAVIG PAGKPIEVQI RTFDMHEEAE
LGVCAHWTYK EGKASRTDAR YENKIAWLRQ VLEWQDDIGD QRIEELAEQI NQAIHDERIY
VFTRDGQVVD LQAGATPLDF AYHIHTEVGH GCRGAKVNGR IVPLTYKLQT GEQVDIMTHR
GGQPSRDWMN PAQGFLASSR SITKVRTWFK QQARDGNVHE GRGLLERELS RLGIGMPKGT
LERLAPRFNL RSAEDVLAAL GAGDLALARI THALSDEQSV AQQELALPEI PVHAPRSDGS
GAGIMIEGVG NLLSHVAGCC KPVPGEPIVG FITQGRGVSI HARGCADYER LAQEDPARTL
DVQWQVGEQA AYPVDIIVRA WDRTGLLRDV TAVLANEQVN VTGVQTQSDK HDATATLRLT
MEVPSLAKLS RVLSRIEQLA MVIEARRLTE HRLPTER
//
