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Database: UniProt
Entry: M7XR02_9BACT
LinkDB: M7XR02_9BACT
Original site: M7XR02_9BACT 
ID   M7XR02_9BACT            Unreviewed;       741 AA.
AC   M7XR02;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EMS30987.1};
GN   ORFNames=C943_02775 {ECO:0000313|EMBL:EMS30987.1};
OS   Mariniradius saccharolyticus AK6.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Mariniradius.
OX   NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS30987.1, ECO:0000313|Proteomes:UP000010953};
RN   [1] {ECO:0000313|EMBL:EMS30987.1, ECO:0000313|Proteomes:UP000010953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK6 {ECO:0000313|EMBL:EMS30987.1,
RC   ECO:0000313|Proteomes:UP000010953};
RA   Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Mariniradius saccharolyticus AK6.";
RL   Submitted (JAN-2013) 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:EMS30987.1}.
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DR   EMBL; AMZY02000026; EMS30987.1; -; Genomic_DNA.
DR   RefSeq; WP_008631881.1; NZ_AMZY02000026.1.
DR   AlphaFoldDB; M7XR02; -.
DR   STRING; 1239962.C943_02775; -.
DR   eggNOG; COG0317; Bacteria.
DR   InParanoid; M7XR02; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000010953; 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; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
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; SM00471; HDc; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EMS30987.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010953};
KW   Transferase {ECO:0000313|EMBL:EMS30987.1}.
FT   DOMAIN          406..467
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   741 AA;  84952 MW;  A9BC63962B138A88 CRC64;
     MIQIDLEEER KEILKRYRKL LKMAKPLLKE GDARIIKKAF SISNDAHKEM RRKSGEPYIY
     HPLEVAMICV EEIGLGTTSI VAALLHDVVE DTDWELEDIE REFGHKVATI IDGLTKISGV
     FEYGSSQQAE NFRKMLLTLS DDVRVILIKL ADRLNNMRTL DSMPRHKQLK IASETMYLYA
     PLAHRLGLYA IKSELEDLYL KFTDSETYRF IANKINETRI SRNRFIKTFI APIEEELESQ
     GFRFTIKGRP KSVFSIYNKM KKQNIPFEEV YDLFAIRIII DSEIDNEKAD CWQVYSIVTD
     FYRPNPDRLR DWISTPRANG YESLHTTVMS NTGQWVEVQI RTVRMDDIAE RGYAAHWKYK
     EKDAAQGGKG PSGLDEWITQ VRSLLESNDG NAIEFMDDFR GNLFHDEVFV FTPKGELKVL
     PHGATALDFA FEIHTEVGAK CIGAKVNTRL VPINHKLKNG DQVEILTSAK QRPTEDWLNS
     VVTSRAKAKI KDALKEEKRS TILDGKEIVQ RKLKQMKMDF NSEIVEQLRA YFETKTPNEF
     YYKIGKGIID PTSIKSFKDF KEQKRQKSKP SLDKVKDESS FTKEIKNLKG PEHDQLLIGE
     DMDVVDYILA KCCNPIPGDD VFGFVTVNEG IKIHRTSCPN ALELLSNHGN RVIKARWTSQ
     QQIAFLAGLR IVGTDRVGLI NDVTKVISNE LKVNMRSITV DSDSGIFEGT IKLYVHSTQH
     LEKLMSNLSK VEGIIKVARF D
//
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