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Database: UniProt
Entry: A0A1I5KD20_9RHOB
LinkDB: A0A1I5KD20_9RHOB
Original site: A0A1I5KD20_9RHOB 
ID   A0A1I5KD20_9RHOB        Unreviewed;       706 AA.
AC   A0A1I5KD20;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   ORFNames=SAMN04488047_10131 {ECO:0000313|EMBL:SFO82907.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFO82907.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFO82907.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFO82907.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
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; FOXA01000001; SFO82907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5KD20; -.
DR   STRING; 441119.SAMN04488047_10131; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000199356; 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; 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; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SFO82907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW   Transferase {ECO:0000313|EMBL:SFO82907.1}.
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"
SQ   SEQUENCE   706 AA;  80264 MW;  2713831D653DC855 CRC64;
     MIDVDDLIAL VRNYNPKTNE GLIREAFDYG QRMHEGQFRH SGEPYFTHPV AVAAILTEMQ
     LDDSTIVTAL LHDVIEDTRS TYGEVVDRFG FEIAELVDGV TKLTNLQLTS TETKQAENFR
     KLFMAMSKDL RVILVKLADR LHNMRTIKSM RHEKQVQKAR ETMDIFAPLA GRMGMQWMRE
     ELEDLAFQVL NPDGRRSIIR RFVTLQRETG DVIDKITTDI RHELDKVGIE AEVFGRAKKP
     FSIWRKMQEK EMGFSRLSDI YGFRVICNSE MDCYGVLGAI HQRWRAVPTR FKDYISQPKS
     NGYRSIHTTV SGRDGKRVEV QIRTREMHEV AETGVAAHWS YRDGVRAENR FAVDPARWIS
     SLTERFHAAE DHDEFLEAVK LEMYQDQVFC FTPKGDVVKL PKGATPLDFA YAIHTRIGDS
     CVGAKVDAIR VPLWTRLKNG QSVEILTAEG QRPQATWIDI VATGRAKTAI RRSLREEDRE
     RFIKLGRELA RVAFDHVGKR VTDKALATAA RQMGLAGSDE VLARLGSAEL TARKVVETLY
     PELARHRGEE VEAQRAVVGL SPEQKYARAQ CCQPLPGERI VGIGYSGRGV VIHAIDCPAL
     EEFESQNDRW VDLHWHSGVH RAVNTVSFDM TISNDAGVLG RICTLIGEQK ANISDLRFVD
     RKPDFYRLIV DVDLRDVEHM HAVMLGLEAD SDVASIVRHR DLGRRP
//
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