ID F2R6X6_STRVP Unreviewed; 804 AA.
AC F2R6X6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=GTP pyrophosphokinase, (P)ppGpp synthetase I {ECO:0000313|EMBL:CCA58755.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:CCA58755.1};
GN OrderedLocusNames=SVEN_5469 {ECO:0000313|EMBL:CCA58755.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58755.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA58755.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC {ECO:0000256|ARBA:ARBA00007476}.
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DR EMBL; FR845719; CCA58755.1; -; Genomic_DNA.
DR AlphaFoldDB; F2R6X6; -.
DR STRING; 953739.SVEN_5469; -.
DR KEGG; sve:SVEN_5469; -.
DR PATRIC; fig|953739.5.peg.612; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_4_1_11; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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 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; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCA58755.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Transferase {ECO:0000313|EMBL:CCA58755.1}.
FT DOMAIN 97..194
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 529..590
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 721..795
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 85185 MW; A78999D3B445E72F CRC64;
MSAEATNPVG AAEAADTDVT VRRRGRARID LRRLGRAALL GATAGPAPRD RLPDAISHVA
EAHRAHHPEA DLSVLRRAYV LAESSHRGQF RKSGEPYITH PLAVTLILAE LGAETTTLTA
SLLHDTVEDT EVTLDQVRRE FGDEVAYLVD GVTKVEKIDY GAAAEPETFR KMLVATGNDV
RVMSIKLADR LHNMRTLGVM RPEKQARIAK VTRDVLIPLA ERLGVQALKT ELEDLVFAIL
HPEEYETTRA LIAGNPQASD ALGAVAEQVA TVLREADIGA EVLVRPRHFV SVHRVRLKRG
ELRGCDFGRL LVLVAEDADC YAVLGELHTC FTPVISEFKD FIAAPKFNLY QSLHTAIAAP
DGAVAEVLIR THRMHTVAEA GVVALGNPHV GQEPAAAPGD LADGDGGAAV APQAHAFRPE
TTSRPGASSR AGSSTRPGAS SRAEASSRPG TSDRSGTTDR RPGADASPGA DASPGADASR
DAAASPAEDG ERVDPTRPGW LSRLLDWQQA APDPDTFWTS LRADLAEDDE ITVFRADGGT
LGLPAGASCV DAAYAQHGEA AHGCLGARVN GRLTPLSTVL GDGDTVQLLL AQDTVSGPSP
EWLDHARTPA ARIAIDGWLR AHPESTAPPA DTSAPRPQAD VPADHRSGAE LHADLEGEPR
AAVRPAGCCT PVPPDKITGF RVRGGSVTVH RAGCAAVDTM RRLGRTPVAV RWGDTAQGRV
TLVAESFGRP GLLADLTEAI AVAGAAVVSA TVEPPSEQRV RHTYTLHLPD VGRLAALMRA
MRDVPGVYDV SRARHRAPSD PRRA
//
