ID A0A1N6JHD6_9FLAO Unreviewed; 734 AA.
AC A0A1N6JHD6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SIO43782.1};
GN ORFNames=SAMN05444409_3418 {ECO:0000313|EMBL:SIO43782.1};
OS Epilithonimonas zeae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=1416779 {ECO:0000313|EMBL:SIO43782.1, ECO:0000313|Proteomes:UP000185207};
RN [1] {ECO:0000313|Proteomes:UP000185207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27623 {ECO:0000313|Proteomes:UP000185207};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FSRK01000003; SIO43782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6JHD6; -.
DR STRING; 1416779.SAMN05444409_3418; -.
DR Proteomes; UP000185207; 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:SIO43782.1};
KW Transferase {ECO:0000313|EMBL:SIO43782.1}.
FT DOMAIN 405..466
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 734 AA; 84431 MW; 8604440F272BF2F5 CRC64;
MMNYDLEKEN KEILARYKDL ISNTYRTLDE ENNKLIRKAF DLALDAHKDQ RRKTGEPYIY
HPIEVAKIVA NEVGLGATSI ACALLHDVIE DSEYTYEDLK KIFGETIADI VNGLTKISVM
NQQNISVQSE NYRKLLLTLS EDFRVILIKI ADRLHNMRTL ESMHPIKQKK IAAETSYIYA
PLAHRFGLYS IKSELEDLSL KYNNPDVYNE ILAKLETAKE GREKYVEEFT KEVSEQLKEE
NLNFTIKGRA KAISSIYRKM QKQNVTFEEV YDNYAIRIIY KSDPRNEKFL AWKIYSIVTD
LYQSNPSRMR DWISQPRSTG YESLHLTVMG PDKKWIEVQI RSERMNEIAE KGVAAHYKYK
EGYRKNTDDQ RFENWVSEIR DVLEQQQNLS TSELLDNIKL NLYSKEVFVF TPKGEIKILP
TGATALDFAF SVHSDLGTKC LGAKINGKLV PISYVLQNGD QIDILSSQNQ KPKADWLEFV
VTSKAKSKIK NILNSEKNQH TAEGKEILQR KMRHAKLNFN EEEINGLQKH LNLKTSQDLF
LGFQNGTFDI GDIKKYADGK SILSNLFQRF RKTSNKEQFV EKVDSNLDMI VFGKDEEKLN
YSFAKCCTVI PGDKIFGFIT ISDGIKVHSE SCPNAINLRA NYDYRVLQAK WVNAESFKNR
IKIEIEGLDR MGMINDITAV ISGSMNMDMK SLSISSNDGI FTGNINLEVK NKSQLEETFK
QLKGIKGVSK VKRV
//
