ID A0A344U3W5_9ACTN Unreviewed; 815 AA.
AC A0A344U3W5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AXE25586.1};
GN ORFNames=C0216_20955 {ECO:0000313|EMBL:AXE25586.1};
OS Streptomyces globosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE25586.1, ECO:0000313|Proteomes:UP000252004};
RN [1] {ECO:0000313|EMBL:AXE25586.1, ECO:0000313|Proteomes:UP000252004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZH-48 {ECO:0000313|EMBL:AXE25586.1,
RC ECO:0000313|Proteomes:UP000252004};
RA Ran K., Li Z., Wei S., Dong R.;
RT "Draft genome Sequence of streptomyces globosus LZH-48.";
RL Submitted (JAN-2018) 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; CP030862; AXE25586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344U3W5; -.
DR KEGG; sgz:C0216_20955; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000252004; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:AXE25586.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000252004};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AXE25586.1}.
FT DOMAIN 118..215
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 473..534
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 737..811
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 90629 MW; CC33F9BCE33179CC CRC64;
MPDEVQPLSA AQPDPQADRA AAPPATPPPA PPAKPAKPAH TRPAPAKSAG SSNRVRARLA
RLGVQRSNPY NPVLEPLLRI VRSNDPKIET ATLRQIEQAY QVAERWHRGQ KRKSGDPYIT
HPLAVTTILA ELGMDPATLM AGLLHDTVED TDYGLEDLRR DFGDAVTLLV DGVTKLDRVK
FGEAAQAETV RKMVVAMAKD PRVLVIKLAD RLHNMRTMRY LKREKQEKKA RETLEIYAPL
AHRLGMNTIK WELEDLSFAI LYPKMYDEIV RLVAERAPKR DEYLAVVIDE VQTDLRAARI
KATVTGRPKH YYSVYQKMIV RGRDFAEIYD LVGIRVLVDT VRDCYAALGT VHARWNPVPG
RFKDYIAMPK FNMYQSLHTT VIGPGGKPVE LQIRTFDMHR RAEYGIAAHW KYKQQTVAGA
SKIRTDVPQA AKGTAGQDTV NDMAWLRQLL DWQKETEDPG EFLDSLRFDL SRNEVFVFTP
KGDVIALPAG ATPVDFAYAV HTEVGHRTIG ARVNGRLVPL ESTLDNGDLV EVFTSKAEGA
GPSRDWLGFV KSPRARNKIR AWFSKERRDE AIEHGKDAIA RAMRKQNLPI QRILTGDSLV
TLAHEMRYPD ISSLYAAIGE GHVAAQGVVQ KLVQALGGEE AANEDIEESV PPSRARTKRR
GSADPGVVVK GVDDVWVKLA RCCTPVPGDP IIGFVTRGSG VSVHRADCVN VDSLSQQPER
ILEVEWAPTQ SSVFLVAIQV EALDRSRLLS DVTRVLSDQH VNILSAAVQT SRDRVATSRF
TFEMGDPKHL GHVLKAVRGV EGVYDVYRVT SARRP
//
