ID A0A0Q6K9T7_9SPHN Unreviewed; 699 AA.
AC A0A0Q6K9T7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ASG67_14570 {ECO:0000313|EMBL:KQU47468.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU47468.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU47468.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU47468.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU47468.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU47468.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQU47468.1}.
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DR EMBL; LMRS01000056; KQU47468.1; -; Genomic_DNA.
DR RefSeq; WP_056532369.1; NZ_LMRS01000056.1.
DR AlphaFoldDB; A0A0Q6K9T7; -.
DR STRING; 1736343.ASG67_14570; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051371; 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:KQU47468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW Transferase {ECO:0000313|EMBL:KQU47468.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 382..443
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 627..699
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 699 AA; 77819 MW; 2DEA355CFA072207 CRC64;
MLRQYELVDR VLDYDPDADE ALLNRAYVFS MHAHGSQKRA SGDPYFSHPI EVAGILTDLR
LDAETIVTAI LHDTVEDTVA TPEEIARLFG PNVARLVDGV TKLSKIEAQT DNERAAENLR
KFLLAMSDDI RVLLVKLADR LHNMRTLHHI AKPEKRRRIA RETMDIYAPL AERVGMYEFM
KEMQTLAFAQ LEPEAFESIT RRLEQLKVGG GDRITRIASG LKLLLSRGGI ESDVTGREKH
PYSIFRKMNE RHISFEQLSD VMAFRALVPT EEDCYRALGV IHRRWPMVPG RFKDYISTPK
RNGYRSLHTT VITAEQTRIE IQIRTPAMHA EADFGLAAHW TYKQAERHDA QVSWIRDLVE
ILDTADSPEE LLEHTRMAMY QDRIFAFTPK GELIQLPKGA TPIDFSYAVH TDLGDQAVGA
KINGRVVPLS TVIENGDQVQ ILRSAGQTPQ PGWLNVAVTG KALAAIRRHL RQTERAEQVT
LGEKLYEDIV ARLPATLGVD AMKQALKRLK LPDEGSLMVA IARRTLSDAA VMEALMPGSA
GADIAAIAPQ SSALSIKGLT PGVAYDLAIC CHPVPGDRIV GLRRPDAGIE VHAIDCVVLT
ELADRSDNET DWVDVSWGER TEGAVARISV TVKNEPGVLG LLATVIGQHR ANIINLRLDT
RDARFHTNAI DVEVHDVQQL MRLIAALRAL DAVNAVERV
//
