ID A0A2K8L4Q2_9PROT Unreviewed; 721 AA.
AC A0A2K8L4Q2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=Ga0123462_1435 {ECO:0000313|EMBL:ATX82298.1};
OS Mariprofundus ferrinatatus.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921087 {ECO:0000313|EMBL:ATX82298.1, ECO:0000313|Proteomes:UP000231637};
RN [1] {ECO:0000313|EMBL:ATX82298.1, ECO:0000313|Proteomes:UP000231637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP-8 {ECO:0000313|EMBL:ATX82298.1,
RC ECO:0000313|Proteomes:UP000231637};
RA McAllister S.M., Kato S., Chan C.S., Chiu B.K., Field E.K.;
RT "Isolation and genomic insights into novel planktonic Zetaproteobacteria
RT from stratified waters of the Chesapeake Bay.";
RL Submitted (DEC-2016) 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 -!- 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; CP018800; ATX82298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8L4Q2; -.
DR KEGG; mfn:Ga0123462_1435; -.
DR Proteomes; UP000231637; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04876; ACT_RelA-SpoT; 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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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:SF40; GTP PYROPHOSPHOKINASE; 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; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ATX82298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231637};
KW Transferase {ECO:0000313|EMBL:ATX82298.1}.
FT DOMAIN 390..453
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 646..721
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 721 AA; 82582 MW; 171457B38E2659F2 CRC64;
MNKTREQHNL TSQYSIPEYI DMLVNHSAHL YQSSPLLEKA CHYVWGAQDV ASELPSSLDV
AILLSHLSAD ETTIIVCLLS DSRLRSPEFH KVIQREFSDE ILQMVRSLEK LHEFRAGKSD
GHEQSERLRR MLLAMVDDVR VVLIKLAYRV QRLRELAKAD TETQKAVASE SLEIFSPIAN
RLGIGQLKWE LEDLSFRYLQ PETYKRIATL LEEKRAGRES YIRQVVTEID TLLKSSDIEA
RVYGRPKHIY SIWSKMTHKN KQFSELFDVL AIRVTVESIA ACYTALGLIH GRWHYIANEF
DDYIANTKAN GYQSLHTAVY GPEGKPVEIQ IRTRAMHEFA EFGVAAHWRY KERTEQDEVL
EKTIHSIRRL LETPENSDEE FLASFKTELF SDRVFVLSPE GKIIDLPQGA TPLDFAYAIH
TEVGHRCRGA KVNGHIVPLT TQLQNGEQVE ILTTNHASPS RDWLNPNLGY ITGSRARSKI
KAWFRQQDYE QNVIDGKTAI DRELKRMHIS NPDTQKLLAH FRVNSEKEWH AKVGRGDITV
RQLTSALNQI YFDDPAQSLP QKPRPKQTGS HDQAIHVCGV GNLLTYMANC CRPVPGDEII
GFITRGKGVS VHRRDCINIL NLEEEKQKRL ISVEWADHEY QTFAITLAIE AIDRTGLLKD
ITSILSDLKV NVVAVQTLSN RDTQTADMQI MMEIEDLEQL QKVSDKIRQL PNVLKVYRQR
A
//
