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Database: UniProt
Entry: A0A024HCY6_PSEKB
LinkDB: A0A024HCY6_PSEKB
Original site: A0A024HCY6_PSEKB 
ID   A0A024HCY6_PSEKB        Unreviewed;       752 AA.
AC   A0A024HCY6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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:CDF82721.1};
GN   ORFNames=PKB_1358 {ECO:0000313|EMBL:CDF82721.1};
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF82721.1, ECO:0000313|Proteomes:UP000025241};
RN   [1] {ECO:0000313|EMBL:CDF82721.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF82721.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Linke B.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDF82721.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF82721.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA   Roy S., Van der Meer J.R.;
RT   "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT   knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL   Submitted (MAY-2014) 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; HG322950; CDF82721.1; -; Genomic_DNA.
DR   RefSeq; WP_043250111.1; NZ_HG322950.1.
DR   AlphaFoldDB; A0A024HCY6; -.
DR   STRING; 1301098.PKB_1358; -.
DR   KEGG; pkc:PKB_1358; -.
DR   PATRIC; fig|1301098.3.peg.1350; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000025241; 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:CDF82721.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000025241};
KW   Transferase {ECO:0000313|EMBL:CDF82721.1}.
FT   DOMAIN          415..476
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          672..747
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   752 AA;  84356 MW;  81DED38560C2CABA CRC64;
     MVQVRAHQPV NTDGSINLEA WLDHVQTLVP VLDRKVLLEA CEFARAAENK AASQVDTAWA
     EGTSSFQTGL EIAEILADLK LDQESLVAAV IYRGVREGKI KLEEVQQRFG SVVAKLIEGV
     LRMAAISTSL NPRQSLVLGT QAQIENLRKM LVAMVDDVRV ALIKLAERTC AIRAVKNADE
     EKRMRVAREV FDIYAPLAHR LGIGHIKWEL EDLSFRYLEP DQYKQIAKLL HERRLDREQY
     IATVMQQLKD ALAATGIKAD LSGRAKHIYS IWRKMQRKGL DFSQIYDVRA VRVLVPEMRD
     CYTALGIVHT LWRHIPKEFD DYIANPKENG YRSLHTAVIG PEGKVLEVQI RTHSMHEEAE
     LGVCAHWRYK GTDVKSGSNH YEEKISWLRQ VLEWHEELGD IGGLAEQLRV DIEPDRVYVF
     TPDGHAIDLP KGSTPLDFAY RVHTEVGHNC RGAKINGRIV PLNYSLQTGE QVEIITGKHS
     GPSRDWLNQN LGYVTTSRAR AKIVHWFKLQ ARDQNVAAGK TMLERELGRL ALPPVDFEKL
     AEKANYKTGE DLFAALGAGD LRLAHVVGYA QALVEPERGN EQLELIPRKP SRIGHGKRGD
     IQIQGVGNLL TQMAGCCQPL PGDPIVGYIT LGRGVTIHRQ DCATVLQLGS REPERMIQVS
     WGPVPVQTYP VDIVIRAYDR SGLLRDVSQV LLNERINVLA VNTRSDKEDN TAVMRLTIEI
     PGLDSLGRLL ARISQLPNII EARRDRAGGK DV
//
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