ID A0A2P2GQU6_9ACTN Unreviewed; 817 AA.
AC A0A2P2GQU6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KKZ73868.1};
GN ORFNames=VO63_10995 {ECO:0000313|EMBL:KKZ73868.1};
OS Streptomyces showdoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68268 {ECO:0000313|EMBL:KKZ73868.1, ECO:0000313|Proteomes:UP000265325};
RN [1] {ECO:0000313|EMBL:KKZ73868.1, ECO:0000313|Proteomes:UP000265325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15227 {ECO:0000313|EMBL:KKZ73868.1,
RC ECO:0000313|Proteomes:UP000265325};
RA Thapa K.K., Metsa-Ketela M.;
RT "Draft Genome assembly of Streptomyces showdoensis.";
RL Submitted (MAY-2015) 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:KKZ73868.1}.
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DR EMBL; LAQS01000013; KKZ73868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2GQU6; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000265325; 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:KKZ73868.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000265325};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKZ73868.1}.
FT DOMAIN 123..220
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 475..536
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 739..813
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 90951 MW; EE84108D6758530D CRC64;
MPDEAQPLSA AQPEQQADQA ASGTAAPQNQ PAEIRPAAPA PAVRPTPASP SRSGGSSSRV
RARLARLGVQ RSSPYNPVLE PLLRIVRSND PKIETATLRQ IERAYQVAER WHRGQKRKSG
DPYITHPLAV TTILAELGMD PATLMAGLLH DTVEDTEYGL DTLRRDFGDQ VALLVDGVTK
LDKVKFGEAA QAETVRKMVV AMAKDPRVLV IKLADRLHNM RTMRYLKREK QEKKARETLE
IYAPLAHRLG MNTIKWELED LAFAILYPKM YDEIVRLVAE RAPKRDEYLA IVTDEVQADL
RAARIKATVT GRPKHYYSVY QKMIVRGRDF AEIYDLVGIR VLVDTVRDCY AALGTVHARW
NPVPGRFKDY IAMPKFNMYQ SLHTTVIGPN GKPVELQIRT FDMHRRAEYG IAAHWKYKQE
AVAGASKVRA DVPKKAGKDD HLNDMAWLRQ LLDWQKETED PSEFLESLRF DLSRNEVFVF
TPKGDVIALP AGATPVDFSY AVHTEVGHRT IGARVNGRLV PLESTLDNGD LVEVFTSKAA
GAGPSRDWLG FVKSPRARNK IRAWFSKERR DEAIEQGKDA IARAMRKQNL PIQRILTGDS
LVTLAHELRY SDISSLYAAI GEGHVTAQSI VQKLVQALGG EEAATEDIEE AAPPARGRSK
RRSNADPGVV VKGVEDVWVK LARCCTPVPG DPIIGFVTRG SGVSVHRSDC VNVDSLSREP
ERILEVEWAP TQSSVFLVAI QVEALDRSRL LSDVTRVLSD QHVNILSAAV QTSRDRVATS
RFTFEMGDPK HLGHVLKAVR GVEGVYDVYR VTSARRP
//
