ID A0A2N7TTE9_9GAMM Unreviewed; 758 AA.
AC A0A2N7TTE9;
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=C1H66_02330 {ECO:0000313|EMBL:PMR71457.1};
OS Halomonas heilongjiangensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1387883 {ECO:0000313|EMBL:PMR71457.1, ECO:0000313|Proteomes:UP000235346};
RN [1] {ECO:0000313|EMBL:PMR71457.1, ECO:0000313|Proteomes:UP000235346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26881 {ECO:0000313|EMBL:PMR71457.1,
RC ECO:0000313|Proteomes:UP000235346};
RA Chen C.;
RT "Halomonas endophytica sp. nov., isolated from storage liquid in the stems
RT of Populus euphratica.";
RL Submitted (JAN-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 -!- 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:PMR71457.1}.
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DR EMBL; PNRE01000015; PMR71457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7TTE9; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000235346; Unassembled WGS sequence.
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; 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: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; PF19296; RelA_AH_RIS; 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:PMR71457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235346};
KW Transferase {ECO:0000313|EMBL:PMR71457.1}.
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 758 AA; 85898 MW; 147AD5688D6AC1B5 CRC64;
MVKVREDQPL SDTGRVDIDQ WIERLQEDVK LRDAAEMREA CQLAQTLERE SDRPHRTWLV
DGSSFRMGLE MADILGELRL DQAALEAAVL YRAVREGLIE LEAVGKRFGE EVAALIGGVL
QMAAISTSQL PSHGMSQHDQ QDNLRKMLVT MIDDVRVALI KIAERTCALR QVKDAPREKC
QRVAREVFDI YAPLAHRLGI GQLKWELEDL SFRYLHEDDY KAIARQLAEK RLDRDRYIHD
VVETLKGMLD AQGIARYDVD GRAKHIYSIW RKMKRKRIDF SQVHDIRAVR ILVPEVADCY
TVLGLVHSRW HHVPNEFDDY IANPKKNGYQ SLHTAVMGPE NKVLEIQIRT FAMHDEAELG
VCAHWRYKGH DTGGKSSSYE EKIAWLRQVL EWQEEVGDFG DIREGLSSDV APDRIYVFTP
DGHVIDLPRI ATPIDFAYRV HTEVGHRCRG AKVNGRIVPL TYKLKTGQQV EILTASKGGP
SRDWLNPSLG YVRTSRARAK IQAWFKHQAR DQNLEEGRAL FDREMKRLDV EGMDLETLAR
KVNYTTPDDM YAALGAGDLR IGQVLHQAQQ LFGESDDQEQ LDRLLAKPRK AAGKGAGSDI
TVLGVGNLKT SMANCCHPVP GESIVGFITQ GRGVTVHRQD CPNILQLRMD EPQRIIEVEW
GERARTQYPV DIEIQAWDRS GLLRDVTGVL SNDKVNVLSV NTLTDTDDGI ARMAITVEVD
GLETLGRLFS RIQQLPNVIE VRRLRSGGKQ GKRRGRSA
//
