ID W0R8M4_BIBTR Unreviewed; 736 AA.
AC W0R8M4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=F544_14370 {ECO:0000313|EMBL:AHG86665.1};
OS Bibersteinia trehalosi USDA-ARS-USMARC-190.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Bibersteinia.
OX NCBI_TaxID=1263832 {ECO:0000313|EMBL:AHG86665.1, ECO:0000313|Proteomes:UP000019086};
RN [1] {ECO:0000313|EMBL:AHG86665.1, ECO:0000313|Proteomes:UP000019086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-190 {ECO:0000313|EMBL:AHG86665.1,
RC ECO:0000313|Proteomes:UP000019086};
RA Harhay G.P., McVey S., Clawson M.L., Bono J., Heaton M.P.,
RA Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT "Annotation of the Bibersteinia trehalosi USDA-ARS-USMARC-190 complete
RT genome.";
RL Submitted (DEC-2013) 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; CP006956; AHG86665.1; -; Genomic_DNA.
DR RefSeq; WP_015432819.1; NZ_CP006956.1.
DR AlphaFoldDB; W0R8M4; -.
DR KEGG; btra:F544_14370; -.
DR PATRIC; fig|1263832.3.peg.1427; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR Proteomes; UP000019086; Chromosome.
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 Kinase {ECO:0000313|EMBL:AHG86665.1};
KW Transferase {ECO:0000313|EMBL:AHG86665.1}.
FT DOMAIN 52..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 397..458
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 661..736
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 736 AA; 83688 MW; 6F5CE45D98D86FFA CRC64;
MVAIRHSHQL DPNNFELASW SAGLKMSPVT FDELQTAWRY AEEKLDTEQL HLMWVGLEMV
EILHGLNMDD DSLVAAMLFP LVKHNIADLA QIKEQFGNGV KNLVKGVLEM ENIRQLNANN
ASDLQIDNIR RMLLAMVDDF RCVVIKLAER IVYLRDTEHH SEEDLVLAAK ECSHIYAPLA
NRLGIGQLKW ELEDYSFRAL HPQDYRQIAK FDLAERRLDR EQFIADFVAH LTACIGEEID
NVQVYGRPKH IYSIWKKMQK KNLRFDQLFD IRAVRIIVQN LEECYTALSI VHSHYKHLPE
HFDDYIADPK PNGYQSLHTV VLGKGDKPIE VQIRTQKMHD DAELGVAAHW KYKEGAGAGR
SGYEEKIVWL RKLLAWQNDI ADSGEMVDDL RSQVFDDRVY VFTPKGEVID LPSNATPLDF
AYSIHSEIGH RCIGAKVAGK IVPFTYILQM GDQVEIITQK NPNPSRDWLN PSQGFVNTPR
ARSKIIAWFK KLDREKNLPI GKEMLESEMV KHQFSLKQIE DYALPRYNLK QLDDLYAAIG
GGDIKLNNLM NYLQGKLVKT SAEQADEAIL KHMAHKAQHT QTKTGRAGAI IVDGVGNLMH
HIARCCQPIP GDKIVGYITQ GRGISIHRAD CEQLFDLQSS SPERVVDAEW GGNFTSGFSL
VIRVIANDRN GLLRDVSAIM ANEKVNVIGV ASRTDIKRSI ATIDIEVELN NIELLDKLLK
RIMQLDDVIE AKRLSN
//
