ID A0A239JX26_9ACTN Unreviewed; 921 AA.
AC A0A239JX26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SNT10229.1};
GN ORFNames=SAMN05443665_101644 {ECO:0000313|EMBL:SNT10229.1};
OS Actinomadura meyerae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=240840 {ECO:0000313|EMBL:SNT10229.1, ECO:0000313|Proteomes:UP000198318};
RN [1] {ECO:0000313|EMBL:SNT10229.1, ECO:0000313|Proteomes:UP000198318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44715 {ECO:0000313|EMBL:SNT10229.1,
RC ECO:0000313|Proteomes:UP000198318};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZOR01000016; SNT10229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239JX26; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000198318; 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:SNT10229.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000198318};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SNT10229.1}.
FT DOMAIN 243..340
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 578..641
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 843..917
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 100423 MW; B6927CD6696D1C22 CRC64;
MPGEAVSTGA VSDTAAAHQA AARSARETAG ERAVKAAGAS TAPARRADRR PPPQPSGPPA
EGPPANGIPA TETSATETSA TETSAAEPDT AETGTAGTPE VEAPAGATAA SAAPATEAPA
DGPQQSAPQQ SDPQQGRPAA RAPRPQSPPA EAPGSTEDAD GASKPDAPSR PTPATIPPSA
ARVRRRLARL GAQRGSAMNP VLEPLIKTVR NTHPKADLRL IERAYDVAAH YHRNQKRKSG
DPYITHPLAV ATILAELGMN TETLCAALLH DTVEDTPYTL DQLSAEFGEE IAALVDGVTK
LDKVKYGEAA EAETVRKMVV AMSRDIRVLV IKLGDRLHNM RTLRYMPRHK QEKKARETLE
VFAPLAHRLG MNTLKWELED LAFATMYPKR FDEIARLVSE RAPRRDVYLQ EVIENVSTDL
RDARIKATVT GRPKHYYSIY QKMIARDVSF DDIYDLVGIR VLVDSVRDCY AALGSIHARW
NPVPGRFKDY IAMPKFNMYQ SLHTTVIGPE GKPVELQIRT WGMHRRAEYG VAAHWKYKEE
TVGGRKAGDM QWLRQLLDWQ KETADPAEFL ESLRFDLSVS EVFVFTPKGD VIALPQGATP
VDFAYAIHTE VGHRCIGARV NGRLVPLESA LDNGDTVEVF TSKSPDAGPS RDWLGFVKSA
RARNKIKHWF SKERRDTAIE SGKDAIARAM RKQNMPLQRM MSGEALLALA RDMRYPDVSS
LYAAVGESQV SAQHVVQRLV DALGGVESAE EDLAEIALPT RRKRGRPAGD PGVVVAGDPD
VWVRLSRCCT PVPGDEIVGF VTRGHGVSVH RADCANVASL KSQPDRLIDV KWSPSEDSVF
LVAIQVEALD RPRLLSDVTR VLSDQHVNIL SASVTTSRDR VAVSRFTFEM GDTKHLGHVL
KAVRSIDGVY DVYRVTSGAT R
//
