ID A0A411WLJ4_9GAMM Unreviewed; 744 AA.
AC A0A411WLJ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=relA {ECO:0000313|EMBL:QBH97109.1};
GN ORFNames=EKN56_12340 {ECO:0000313|EMBL:QBH97109.1};
OS Limnobaculum zhutongyuii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Limnobaculum.
OX NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH97109.1, ECO:0000313|Proteomes:UP000293154};
RN [1] {ECO:0000313|EMBL:QBH97109.1, ECO:0000313|Proteomes:UP000293154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF-458 {ECO:0000313|EMBL:QBH97109.1,
RC ECO:0000313|Proteomes:UP000293154};
RA Ge Y.;
RT "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL Submitted (MAR-2019) 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; CP034752; QBH97109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WLJ4; -.
DR KEGG; prag:EKN56_12340; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000293154; 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; 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: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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:QBH97109.1};
KW Transferase {ECO:0000313|EMBL:QBH97109.1}.
FT DOMAIN 55..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 668..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 569..596
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 744 AA; 84627 MW; 951EA8E53233F545 CRC64;
MVAVRSAHLN TAGEFELDKW IGILGINSPE LCERLAATWR YCEQQVQGNP DASLLLWRGL
EVVEILATLS MDNESMRAAL LFPLADAKII DEETVKEQFG SEVANLVHGV LDMDAIRQLN
ATHNGSNTSI QVDNVRRMLL AMVEDFRCVV IKLAERIAHL REVKDEAEEV RVLAAKECFN
IYAPLANRLG IGQLKWEMED FCFRYLHPAE YKQIANLLHE RRIDREVYID TFVQTLRDSM
KEQGIQGVIY GRPKHIYSIW RKMQKKALAF EELYDVRAVR IVVERLQDCY AALGIVHTHF
RHLPSEFDDY VANPKPNGYQ SIHTVVFGPK GHAVEIQIRT RQMHEDAELG VAAHWKYKEG
STVSGRSGYE ERIAWLRKLI AWQEEMSDSG EMLDEVRSQV FDDRVYVFTP KGDVIDLPTG
STPLDFAYHI HSDVGHRCIG AKIGGRIVPF TYQLQMGDQI EIITQKQPNP SRDWLNPNLG
FVNSSRARAK IQAWFKKQDR DKNILAGRQI LDDELERLSI SFKDAEKLLV PRYNVHSFDE
VLAGIGGGDI RLNQLVNFLQ SKFNQPTAEE ADREALRQLN QKTANAQQRN AKNNSQIVVE
GVGNLMHHIA RCCQPIPGDD IVGFITQGRG ISIHRSDCDQ LNELKNHAPE RLVEAVWGDF
YSSGYSLVVR VVANDRSGLL RDITTILANE KVNVLSVSSR SDVKKQMATI DMEIELYNLQ
VLDRVLSRIN QLPDIIEAKR LGVK
//
