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Database: UniProt
Entry: A0A0P1FZ10_THAGE
LinkDB: A0A0P1FZ10_THAGE
Original site: A0A0P1FZ10_THAGE 
ID   A0A0P1FZ10_THAGE        Unreviewed;       710 AA.
AC   A0A0P1FZ10;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN   Name=rsh {ECO:0000313|EMBL:CUH66287.1};
GN   ORFNames=TG4357_02349 {ECO:0000313|EMBL:CUH66287.1};
OS   Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH66287.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH66287.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH66287.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-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}.
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DR   EMBL; CYSA01000023; CUH66287.1; -; Genomic_DNA.
DR   RefSeq; WP_058263087.1; NZ_FOFW01000004.1.
DR   AlphaFoldDB; A0A0P1FZ10; -.
DR   STRING; 53501.SAMN04488043_10480; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000051587; 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; 2.
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:CUH66287.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW   Transferase {ECO:0000313|EMBL:CUH66287.1}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          382..447
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          627..701
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   710 AA;  79760 MW;  4813FEE37CD252BE CRC64;
     MIAVDDLIAL VCNYNPKTNE NLLREAYAFG LAMHEGQFRH SGEPYFTHPV AVAAILTEQR
     LDDATIVTAL LHDTVEDTKA SYSEVEKRFG KEIADLVDGV TKLTNLQLSS SETKQAENFR
     KLFMAMSKDL RVILVKLADR LHNMRTIKAM RPDKQSQKAR ETMEIYAPLA GRMGMQSMRE
     ELEDLAFKVL NPEARASIMR RFVMLQNETG DVIHRITGDM RQELDEVGID AQVFGRAKKP
     YSIWRKMSEK DVGFSRLSDI YGFRVITNSE DDCYRALGVI HQRWRAVPGR FKDYISQPKS
     NGYRSIHTTV SGRDGKRVEV QIRTRQMHDV AETGVAAHWS YRDGVRAMNP FAVDPAKWLA
     GLTEQFNAEE DHDAFLEAVK LEMYTDKVFC FTPKGEVVKL PKGATPIDFA YAIHTRIGNA
     CVGAKIDGMR VPLWTRVKNG QSIEIITAEG QTPQATWLDI ATTGKARTAI RRALREVDRE
     RFSKLGRELA RSAFDHVGKK ATDKALETAA RNLRLEDTDM LLALLGSAEL TTRDVLHAVY
     PELSEAESDD IELRGAVVGL SHDQHFTIAR CCQPLPGERI VGISHRGKGV IVHAIDCEAL
     ANYEDQPNRW MDLHWHAGKH PAIHATTLNV TIGNDAGVLG RICTLIGEQK ANIADLVFVD
     RKPDFFRLLI EIELRDAEHL HSVMSALEAE SDVAAVQRHR DPTRANMQAG
//
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