ID A0A2A9EH58_9MICO Unreviewed; 779 AA.
AC A0A2A9EH58;
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:PFG37956.1};
GN ORFNames=ATJ97_0424 {ECO:0000313|EMBL:PFG37956.1};
OS Georgenia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=638953 {ECO:0000313|EMBL:PFG37956.1, ECO:0000313|Proteomes:UP000222106};
RN [1] {ECO:0000313|EMBL:PFG37956.1, ECO:0000313|Proteomes:UP000222106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21838 {ECO:0000313|EMBL:PFG37956.1,
RC ECO:0000313|Proteomes:UP000222106};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
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:PFG37956.1}.
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DR EMBL; PDJI01000004; PFG37956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9EH58; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000222106; 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:PFG37956.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000222106};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PFG37956.1}.
FT DOMAIN 83..180
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 425..488
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 692..769
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 85964 MW; 3D8F86322645C569 CRC64;
MAGDRVPAAG EGSGTDTVVP GSRVRSRLVW LGSRGHSSPP AIEPLLRAVR ANHPKADTQL
IVRAYEVAEK AHRGQMRKSG DPYITHPVAV ATILAELGMT PSTLAAALLH DTVEDTDYPL
EQLRSEFGDE IALLVDGVTK LDKVTYGDAA QAETVRKMVV AMAKDIRVLV IKLADRLHNA
RTWKYVPAAS AERKARETLE IYAPLAHRLG MNTIKWELED LSFATLYPKV YEEIVHLVAE
RAPARDEYLR TVRLQIEDDL RTARIKGIVT GRPKHYYSIY QKMIVRGRDF DDIFDLVGVR
VLVDTVRDCY AALGAMHARW TPLPGRFKDY IAMPKFNLYQ SLHTTVVGPG GKPVEIQIRT
HDMHRRAEYG VAAHWKYKEN PNTKGGKAET PLATEEMGWL RQLVDWQRET ADPGEFLDSL
RFEMSGAQVY VFTPKGDVMA LPSGATPVDF AYAVHTEVGH RTVGARVNGK LVPLDSMLEN
GDTVEIFTSR SEGAGPSQDW LTFVKSPRAR NKIKAWFTKE RREEAIEAGK NQLGKAMRKQ
NLPIQRLMSH DSLSALATEM RYADVSALYA AIGENHISAT NVVQKLVQSM GGESGAEETL
AEATMPGEHR PRARTGDTSV VVEGMSDTDI WVKLARCCTP VPGDPIVGFI TRGSGVSVHR
ADCGNLEGLR SQPERMVGVS WAKSAQSSFL VQIQVEALDR NGLLSDVTRV LSENHVNILS
ASVSTSRDRV ALSKFVFEMA EPSHLGHVLA AVRKIDGVFD AYRVTGTRSA RTPAPDLGR
//
