ID A0A0D8CKW4_9PROT Unreviewed; 714 AA.
AC A0A0D8CKW4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
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};
GN ORFNames=UF64_00765 {ECO:0000313|EMBL:KJE36920.1};
OS Thalassospira sp. HJ.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE36920.1, ECO:0000313|Proteomes:UP000032356};
RN [1] {ECO:0000313|EMBL:KJE36920.1, ECO:0000313|Proteomes:UP000032356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJ {ECO:0000313|EMBL:KJE36920.1,
RC ECO:0000313|Proteomes:UP000032356};
RA Kiseleva L., Garushyants S.K., Goryanin I.;
RT "Complete genome of Thalassospira sp. strain HJ.";
RL Submitted (FEB-2015) 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:KJE36920.1}.
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DR EMBL; JYII01000003; KJE36920.1; -; Genomic_DNA.
DR RefSeq; WP_044826725.1; NZ_JYII01000003.1.
DR AlphaFoldDB; A0A0D8CKW4; -.
DR STRING; 1616823.UF64_00765; -.
DR PATRIC; fig|1616823.3.peg.3468; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000032356; 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:SF36; 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; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KJE36920.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032356};
KW Transferase {ECO:0000313|EMBL:KJE36920.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 640..714
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 714 AA; 80874 MW; 513E8B09CA5BBAF8 CRC64;
MMRQYELVER VKAYDPDACE TTLNRAYVYA TQKHGSQKRA SGDPYFSHPI EVAGILTNYK
LDCDTIITAL LHDTIEDTDA TPEEITKLFG SNIMKLVDGV TKLTQIELKS ADSKQAENFR
KLLLAMSEDI RVLLVKLADR LHNMRTLHYI SKPEKRVRIA AETLEIYAPL AERIGMHDIK
EELEDLAFQH INPEARDSIL ARLEFLRQKD DNVVSRIVSE LTDVVSRQGL KVDIYGREKR
PYSIWQKMQR KNITFGELSD IMAFRVLVED MPQCYEVLGY LHANYKVVPG RFKDYISTPK
PNGYRSIHTT VLGPENHRIE VQIRTRQMHE VNENGVAAHW AYKQETPTGE QKEGVQYRWL
RDLLDILEHA SEPEEFLEHT KLAMFQDQVF CFSPKGDVIA LPARATPVDF AYMIHTHIGD
TCVGAKVNGA MVPLRTVLNN GDQVEIVTSK AQTPNPTWER FVVSGKARAR IRRFIRQQQE
DQYKDLGKAI LQKAFRQEGY DYSDKALEGV LKIFKQPSVE ALLTLVGAGH HTGREVVHAV
FPGTKDKETA RKVVPLDKVR ARKHEHAIPI KGLIPGMAVH YAGCCHPLPG DRIVGIVTTG
KGVTIHTIDC DTLETFTEQP ERWLDVGWDN EGEPEHFIGR LGLTVGHEQG ALSSITSVIA
KNHGNITNLR FTNRTTDFFE MLIDIDVVDV KHLTNIIAAL RATPVVNAVE RARG
//