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Database: UniProt
Entry: K2EZS3_9BACT
LinkDB: K2EZS3_9BACT
Original site: K2EZS3_9BACT 
ID   K2EZS3_9BACT            Unreviewed;       469 AA.
AC   K2EZS3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EKE11099.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:EKE11099.1};
GN   Name=relA {ECO:0000313|EMBL:EKE11099.1};
GN   ORFNames=ACD_15C00138G0022 {ECO:0000313|EMBL:EKE11099.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE11099.1};
RN   [1] {ECO:0000313|EMBL:EKE11099.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKE11099.1}.
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DR   EMBL; AMFJ01005795; EKE11099.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2EZS3; -.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; cd05399; NT_Rel-Spo_like; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007685; RelA_SpoT.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EKE11099.1};
KW   Transferase {ECO:0000313|EMBL:EKE11099.1}.
FT   DOMAIN          224..337
FT                   /note="RelA/SpoT"
FT                   /evidence="ECO:0000259|SMART:SM00954"
SQ   SEQUENCE   469 AA;  55157 MW;  075341BB8FE4635E CRC64;
     MVSNKNIAQN KFKNRTEKTL DSSQRFLNTL KRKKANGYTQ NGVLLMKTLK EITNDPSLLS
     ICLFYDVLNY PEGKKILKNS NLSKSEQIII KKLHSLENLS IDSNIKDINK ALRYFSADYR
     ILILRITHRL LDIRNLEKFS QKKAKKIAQE TLHMYVPLAS RLGLHKWRHE MEDICFKYLF
     PRIAKKLERK FDFYRENDIS CLKHTEKYIK QKLTESGIKC TLENRIKSIY STYRKMIVKN
     RKFDELTDRL AIRIIVAKKD TCYRALGVIH SIMHPIPGKF KDYIGTPKEN GYQSIHTVVF
     PLPNVTNMPI EIQIRSKEMH KECEFGVASH FHYKKDSYTM RYNKKTRADL IKNLEIIKHE
     SPTSTQKLSH LMQSYFRGDQ VLVFDSKNRV YHLTKPASAL DFVCIHYKKK IAYLKSVKIN
     GILGSLETLL QDGDVVEAQF QEKKSFSKRW IKMCHREQSK KMLLEISNE
//
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