ID Q48FH8_PSE14 Unreviewed; 744 AA.
AC Q48FH8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
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:AAZ33607.1};
GN OrderedLocusNames=PSPPH_3716 {ECO:0000313|EMBL:AAZ33607.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ33607.1, ECO:0000313|Proteomes:UP000000551};
RN [1] {ECO:0000313|EMBL:AAZ33607.1, ECO:0000313|Proteomes:UP000000551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000058; AAZ33607.1; -; Genomic_DNA.
DR AlphaFoldDB; Q48FH8; -.
DR KEGG; psp:PSPPH_3716; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR Proteomes; UP000000551; 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; 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:AAZ33607.1};
KW Transferase {ECO:0000313|EMBL:AAZ33607.1}.
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 668..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 744 AA; 83570 MW; 1EF481B60368E3DF CRC64;
MRANQPINTD GSINLDAWLD HIVSVDLVLD REVMKQACEF ARQAEQNDKA HKNHWAEGTS
SFQTGLEIAE ILADLKLDQD SLVAAVIYRG VREGVIPLPE VEQRFGATVA KLIDGVLRMA
AISASLSPRQ SLVLGSQAQV ENLRKMLVAM VDDVRVALIK LAERTCAIRA VKNADDEKRN
RVAREVFDIY APLAHRLGIG HIKWELEDLS FRYLEPDQYK QIAKLLHERR LDRERFISDV
MSQLDNELQA TGVTADISGR AKHIYSIWRK MQRKGLAFSQ IYDVRALRVL VPEMRDCYTA
LGIVHTLWRH IPKEFDDYIA NPKENGYRSL HTAVIGPEGK VLEVQIRTHA MHEEAELGVC
AHWRYKGTDV KSGSNHYEEK ISWLRQVLEW HEELGDIGGL ADQLRVDIEP DRVYVFTPDG
HAIDLPKGAT PLDFAYRVHT EIGHNCRGAK INGRIVPLNY SLQTGEQVEI ITSKHGTPSR
DWLNSNLGYI TTSRARAKIV HWFKLQARDQ NVAAGKTLIE RELARLALPQ VDFDKLADKA
NHKTADDMFA ALGAGDLRLA QLVNLAQQQV EPDRVNEQLE LIPRKATGYK PGKRGDIQIQ
GVGNLMTQMA GCCQPLPGDA IVGYITQGRG VSIHRQDCAS VLQLGGREPE RIIQVSWGPV
PVLTYPVDII IRAYDRSGLL RDVTQVLLNE RINVLAVNTR SNKEDNTALM SLTIEIPGLD
ALGRLLGRIS QLPNIIETRR NRTP
//
