ID A0A1T4PWH2_9ENTE Unreviewed; 741 AA.
AC A0A1T4PWH2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=SAMN02745116_01948 {ECO:0000313|EMBL:SJZ95657.1};
OS Pilibacter termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX NCBI_TaxID=263852 {ECO:0000313|EMBL:SJZ95657.1, ECO:0000313|Proteomes:UP000190328};
RN [1] {ECO:0000313|EMBL:SJZ95657.1, ECO:0000313|Proteomes:UP000190328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SJZ95657.1,
RC ECO:0000313|Proteomes:UP000190328};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXI01000023; SJZ95657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4PWH2; -.
DR STRING; 263852.SAMN02745116_01948; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000190328; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP 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:0003723; F:RNA binding; 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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SJZ95657.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000190328};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SJZ95657.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..741
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 741 AA; 84821 MW; EA1E159FCE2A50C4 CRC64;
MSKEENMTGE EVIRMVSHYM TEEQTQFVQK ALDFATEKHA PDTRKSGEPY IIHPIQVAGI
LAELHMDAHT VATGFLHDVV EDTPVTLEDL KEFFGDDVAN LVDGVTKLGK IKYKSHEEQL
AENHRKMLIA MAQDLRVILV KLADRLHNMR TLEHLREDKQ RRISMETMEI YAPLAHRLGI
SRIKWELEDT ALRYLNPQQY YRIVNLMNSK RTEREEYIAD SVEQIREATE ELEIYAEIYG
RPKHLYSIYR KMKDQKKQFE EIYDLLAIRV IVDSIKECYA VLGAIHTKWT PMPGRFKDYI
AMPKANMYQS IHTTVIGPNG NPLEVQIRTT EMHEVAEFGV AAHWAYKEGQ TKKLKEDAMT
KTLSWFHEIL DLQKESTDAT DFIESVKGDI FSDKVYVFTP KGEVTELPAG SGPLDFAYSI
HTQIGDKTTG AKVNGKMVQL DYKLKTGDII EIITSSNSFG PSRDWLKLVK TTKARNKIKR
FFKTQDKELS INKGREMIVH ELVEMKFNTA VYLNKAHVTE ILERFNYKTE EELFAAVGFG
EISPITVANR LTEKERRAID KQKQKEKEDA LLHNAVKVEK EPEKMKIRHE GGIIIQGASN
LMVRLSRCCN PVPGDEIIGY ITKGRGISIH RKDCQNLASQ PELNERTIDV EWEDSRISNN
GKDYVAELDI FGYNRSGLLN DILQVISGQT KNLVSVEAKP TKEKMATIHV ALGIKDIHHL
TAIVDKIKSV PDVYSVKRTN G
//
