ID A0A0N9W0X9_9GAMM Unreviewed; 767 AA.
AC A0A0N9W0X9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AOY20_06295 {ECO:0000313|EMBL:ALH95176.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95176.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH95176.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH95176.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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}.
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DR EMBL; CP012808; ALH95176.1; -; Genomic_DNA.
DR RefSeq; WP_054581070.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9W0X9; -.
DR STRING; 1324350.AOY20_06295; -.
DR KEGG; aei:AOY20_06295; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000064939; Chromosome.
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:ALH95176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064939};
KW Transferase {ECO:0000313|EMBL:ALH95176.1}.
FT DOMAIN 429..492
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 691..765
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 767 AA; 88231 MW; BDBDC42445AB7C5E CRC64;
MVTVREQLPG RLTELSEETT VEHAEQARQD IAKWLDRVRD ILDGAALKRL EEVASYTLQK
ELETTVSHRS NTLYTGIEMA DILAHLHVDE DTLSASLLYR GVREGVIPLE DVKELFGEGV
YGLVKGTLAM GKLSDLIEKN KRLEDHFNNN QREHLTGIYK MLISVTEDVR VVLIKLAERT
FALRELAHSS KERQERVARE ILTIYAPLAH RLGIAQLKWE LEDLAFRYLA PDRYKEIASL
LNEKRLEREQ YIQFVIDKLK NELAENGIEA EINGRVKHIY SIYRKMKSKN LSFDQLYDIR
AVRVLVKSVP ECYHSLGIVH QIWRHIPHQF DDYITNPKAN GYRSLHTAVI AENKSLEVQI
RTKDMHEEAE LGVCSHFNYK EGAKTTDRSF NHRLHSLRSV LEHYQERNDA SAHKDEDVDD
FEQIQEFEDF EKIYVFSRDG DIKELPRGST VLDFAFHVHT EVGNKCYAAR VNQRYVPLTY
TLKTGEQVEI LTKKDREPNR DWLVNSLGYI KTARARDKLR HWFRQQDRSK NLEVGREILN
KELSRLAIHP KSIDLNDYCN HFNVKHGEDI LIGLVSGDIS LHSLINQVNR HMHLDQDEPE
LVLKPALNPR ASHTLSAHGI LIDGLDNVEL HVAQCCQPVH GESIAGYITL NRGVSIHKVI
CSDYVRMISQ EPERAVEADW EMQPTRGQSV QIVVEAYDRR GLLKDLTQVI FADQINIRQV
NTISEADGIA NMKLLIEVKG LAQLSKLLAR LEQQPGIISA RRLVQGN
//
