ID A0A316BG70_9MICO Unreviewed; 750 AA.
AC A0A316BG70;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PWJ61573.1};
GN ORFNames=B0H03_11649 {ECO:0000313|EMBL:PWJ61573.1};
OS Rathayibacter iranicus NCPPB 2253 = VKM Ac-1602.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1328868 {ECO:0000313|EMBL:PWJ61573.1, ECO:0000313|Proteomes:UP000245674};
RN [1] {ECO:0000313|EMBL:PWJ61573.1, ECO:0000313|Proteomes:UP000245674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1602 {ECO:0000313|EMBL:PWJ61573.1,
RC ECO:0000313|Proteomes:UP000245674};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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}.
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:PWJ61573.1}.
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DR EMBL; QGDV01000016; PWJ61573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316BG70; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000245674; 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:PWJ61573.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PWJ61573.1}.
FT DOMAIN 71..168
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 675..749
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 576..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 83604 MW; 0EE052CD84D4E226 CRC64;
MTETTSTSST AALRRLVPRI FSRAQPSGAV DTLVRTVRTH HPKSDIALIE RAYSVAERAH
SSQKRRSGEP YITHPLAVAQ ILADLGIGSK TIAAALLHDT VEDTDYTLDE LRADFGDEVA
MLVDGVTKLD KVKYGDSAQA ETVRKMIVAM SKDIRVLIIK LADRLHNART WGFVPAESAA
RKATETLEIY APLAHRLGIQ AIKWELEDLS FAVLYPKIYN EIESLVKRRT PQREEFVQSV
IDLISEDLRA GRIRGRVVGR PKQYYSIYQK MVVRGREFDE IYDLVGIRVL VNSVRDCYAV
LGSIHARWTP IPGRFKDYIA TPKFNLYQSL HTTVVGPKGR AVEIQIRTNE MHQHAEFGIA
AHWKYKEQMA TGKVPISGSN DNDLAWLAHL SDWQSETTDP NEFLDSLRFE IGAKEVYVFT
PKGRVIGLPT GATPVDFAYA VHTEVGHRTM GAKVNGRLVP LESSLTTGDV VEVFTSKNPD
SGPSQDWLHF VQSPRARNKI RQWFTKERRD EAIEQGKDSI ARAMRKQNLP LQKLMSQDTF
TEVASQLRYN DVEALYAAVG EGHVSTQSVL EKVVSSIQGD PESDENEVTL PRSPRPRSRS
SESGVLVKGA PDILVKLAKC CTPVPGDQIV GFVTRGAGVS VHQANCHNVQ ELLKEPERIV
DVEWAPSSKS IFLVQIQVEA LDRSGLLSDV TRVLSEHHVN ILSATVSTSS DRLAISRFVF
EMGDTTHLDR VLNAVRRIDA VYDVYRVSAG
//
