ID A0A2B8B086_9ACTN Unreviewed; 854 AA.
AC A0A2B8B086;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PGH51361.1};
GN ORFNames=CRI70_07010 {ECO:0000313|EMBL:PGH51361.1};
OS Streptomyces sp. Ru87.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH51361.1, ECO:0000313|Proteomes:UP000222409};
RN [1] {ECO:0000313|EMBL:PGH51361.1, ECO:0000313|Proteomes:UP000222409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru87 {ECO:0000313|EMBL:PGH51361.1,
RC ECO:0000313|Proteomes:UP000222409};
RA Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA Wellington E.M.H.;
RT "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT soil.";
RL Submitted (OCT-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}.
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:PGH51361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDIX01000096; PGH51361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8B086; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000222409; Unassembled WGS sequence.
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:PGH51361.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000222409};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PGH51361.1}.
FT DOMAIN 158..255
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 513..574
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 776..850
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 94475 MW; 1AEA4760AA1BEFCD CRC64;
MPDEAKPLAP GLRPGESPAA QPARPAEAAA APDAPPRDDA AAAGTSGRPT TPAAPVTRPK
PPAGGRQNGT AKPVGAGPVG PAQSPAPRTG SSNRVRARLA RLGVQRSSPY NPVLEPLLRI
VRSNDPKIEA ATLRQVEQAY QVAERWHRGQ KRKSGDPYIT HPLAVTTILA ELGMDPATLM
AGLLHDTVED TEYGLDTLRR DFGDQVALLV DGVTKLDKVK FGEAAQAETV RKMVVAMAKD
PRVLVIKLAD RLHNMRTMRY LKREKQEKKA RETLEIYAPL AHRLGMNTIK WELEDLAFAI
LYPKMYDEIV RLVAERAPKR DEYLAVVTDE VQADLRAARI KATVTGRPKH YYSVYQKMIV
RGRDFAEIYD LVGIRVLVDT VRDCYAALGT VHARWNPVPG RFKDYIAMPK FNMYQSLHTT
VIGPSGKPVE LQIRTFDMHR RAEYGIAAHW KYKQEAVAGA SKVRTDVPRR TGKDADKDAV
NDMAWLRQLL DWQKETEDPS EFLESLRFDL SRNEVFVFTP KGDVIALPAG ATPVDFAYAV
HTEVGHRTIG ARVNGRLVPL ESTLDNGDLV EVFTSKAPGA GPSRDWLGFV KSPRARNKIR
AWFSKERRDE AIEQGKDSIA RAMRKQNLPI QRILTGDSLV TLAHELRYPD ISSLYAAIGE
GHVTAQNIVQ KLVHALGGED ETNEDLAEST PMRSRAKRRA KNDPGVVVKG VDDVWVKLAR
CCTPVPGDPI IGFVTRGSGV SVHRADCVNV DSLSQQPERI LEVEWAPTQS SVFLVAIQVE
ALDRSRLLSD VTRVLSDQHV NILSAAVQTS RDRVATSRFT FEMGDPKHLG HVLKAVRGVE
GVYDVYRVTS TKRP
//
