ID D6EPR5_STRLI Unreviewed; 847 AA.
AC D6EPR5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EFD70403.2};
GN ORFNames=SSPG_06043 {ECO:0000313|EMBL:EFD70403.2};
OS Streptomyces lividans TK24.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD70403.2};
RN [1] {ECO:0000313|EMBL:EFD70403.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TK24 {ECO:0000313|EMBL:EFD70403.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces lividans strain TK24.";
RL Submitted (FEB-2009) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; GG657756; EFD70403.2; -; Genomic_DNA.
DR RefSeq; WP_003977314.1; NZ_GG657756.1.
DR AlphaFoldDB; D6EPR5; -.
DR SMR; D6EPR5; -.
DR HOGENOM; CLU_012300_3_0_11; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000002769; Unassembled WGS sequence.
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:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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:EFD70403.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFD70403.2}.
SQ SEQUENCE 847 AA; 94182 MW; 544040B21A0D512E CRC64;
MPDEAQPLTA AKPESASASA AKPAPSAPQA KNDTHGPIQH APAAPVDKPA EQQPRPKPLP
AERPQNAPVV RAPAGQPARS GSSNRVRARL ARLGVQRANP YNPVLEPLLR IVRGNDPKIE
TSTLRQIERA YQVAERWHRG QKRKSGDPYI THPLAVTTIL AELGMDPATL MAGLLHDTVE
DTEYGLEDLR RDFGDVVTLL VDGVTKLDKV KFGEAAQAET VRKMVVAMAK DPRVLVIKLA
DRLHNMRTMR YLKREKQEKK ARETLEIYAP LAHRLGMNTI KWELEDLAFA ILYPKMYDEI
VRLVAERAPK RDEYLAVVTD EVQQDLRAAR IKATVTGRPK HYYSVYQKMI VRGRDFAEIY
DLVGIRVLVD TVRDCYAALG TVHARWNPVP GRFKDYIAMP KFNMYQSLHT TVIGPGGKPV
ELQIRTFDMH RRAEYGIAAH WKYKQEAVAG ASKVRTDAPK SSGKSKDDHL NDMAWLRQLL
DWQKETEDPG EFLESLRFDL SRNEVFVFTP KGDVIALPAG ATPVDFAYAV HTEVGHRTIG
ARVNGRLVPL ESTLDNGDLV EVFTSKAAGA GPSRDWLGFV KSPRARNKIR AWFSKERRDE
AIEQGKDAIV RAMRKQNLPI QRILTGDSLV TLAHEMRYSD ISALYAAIGE GHVSAPNIVQ
KLVQALGGEE AATEEIDESV PPSRGRGRKR RANADPGVVV KGVEDVWVKL ARCCTPVPGD
PIIGFVTRGS GVSVHRSDCV NVDSLSREPE RILEVEWAPT QSSVFLVAIQ VEALDRSRLL
SDVTRVLSDQ HVNILSAAVQ TSRDRVATSR FTFEMGDPKH LGHVLKAVRG VEGVYDVYRV
TSARRPS
//
