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Database: UniProt
Entry: A0A1G9P872_9SPHI
LinkDB: A0A1G9P872_9SPHI
Original site: A0A1G9P872_9SPHI 
ID   A0A1G9P872_9SPHI        Unreviewed;       743 AA.
AC   A0A1G9P872;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SDL94988.1};
GN   ORFNames=SAMN05421813_10428 {ECO:0000313|EMBL:SDL94988.1};
OS   Daejeonella rubra.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=990371 {ECO:0000313|EMBL:SDL94988.1, ECO:0000313|Proteomes:UP000199226};
RN   [1] {ECO:0000313|Proteomes:UP000199226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24536 {ECO:0000313|Proteomes:UP000199226};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNHH01000004; SDL94988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9P872; -.
DR   STRING; 990371.SAMN05421813_10428; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000199226; 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; IPR006674; HD_domain.
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; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SDL94988.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199226};
KW   Transferase {ECO:0000313|EMBL:SDL94988.1}.
FT   DOMAIN          60..159
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          403..464
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   743 AA;  84755 MW;  BD47C0C042820FC0 CRC64;
     MKELVIDIEA EKKEILKRYR ALLRACKSTM QKGDKRMIRL AFDMALASHQ NMRRKSGEPY
     IYHPIAVAQI AAEEIGLGTT SIVCALLHDV VEDTDITLDD IEREFGKKVA KIIDGLTKIS
     GVFDYNSSLQ AENFRKMLLT LADDVRVILI KLADRLHNMR TMDFMPRDKQ LKISSETVYL
     YAPLAHRLGL YTLKSELEDL AMKYMEPVTY KFIAQQLNEK KAERENFIRD FITPIKEILN
     EQGLDADLYG RPKSIHSIWT KMRKKNIPFD EVYDLFAIRI ILNSKPESEK SDCWKAYSIV
     TDLYRPNPDR LRDWISSPRA NGYESLHTTV MGPRGQWVEV QIRTNRMNEI AEKGFAAHWK
     YKEEPNTDSG LDQWIHKVRE LLSNPEANAL DFLDDFKMNL FSDEIFIFTP KGALIQLPVE
     ATALDFAFEI HTDIGASCIG AKVNHKLVPL SHKLQNGDQV EIITSGKQSP KEDWLSFVVT
     AKAKSKIKSS LKEEKRKIAE QGKEILERKL KSLKVTYNTD NLYKLSYYFK LSSTLDLFYN
     VAQGKIDVKQ LKEFVASEKV VENKPEKIDN GYNEQLIKKV KGDDNDTLLI GEDLQKLDYK
     LSSCCNPIPG DDVFGFVTVG DGIKIHRTNC PNAAKLMSNY GYRIVKARWN SQKELAFLTG
     LHITGIDDVG LINKITTVIS SDFKVNMRSI TVDTDNGIFE GSIMVYVNNT KHLDNLINKL
     KEVVGVTSVT RFDSNPEDLV KAS
//
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