ID Q5WW82_LEGPL Unreviewed; 734 AA.
AC Q5WW82;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
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:CAH15811.1};
GN OrderedLocusNames=lpl1571 {ECO:0000313|EMBL:CAH15811.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH15811.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH15811.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH15811.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH15811.1; -; Genomic_DNA.
DR RefSeq; WP_011215608.1; NC_006369.1.
DR AlphaFoldDB; Q5WW82; -.
DR KEGG; lpf:lpl1571; -.
DR LegioList; lpl1571; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR Proteomes; UP000002517; 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; 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:CAH15811.1};
KW Transferase {ECO:0000313|EMBL:CAH15811.1}.
FT DOMAIN 407..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..734
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 734 AA; 83263 MW; 8A0BF11FD55F0FE2 CRC64;
MVRVKDTTPL TADGSIDVEM WLHHLGSKGY LDNLELVRAA CTLSQLAGQD HATETGQTCL
QQGLSMADLL ADLEVDQETL AAAIIFENVH YADLSIDDVE EQLGHNIAKL VKGIEKMSAM
NNFQALNKYP QNKNQIDNIR KMLLAMVDDV RVVLIKLAEC LCILRTAGHL SETIRKQLAT
EAMEIYAPLA NRLGIGAIKW EMEDLAFRHL HPEEYKAIAK GLKAKRLERD SFVNRIVEQL
EHQIRATGAR HFAVYGRSKH IHSIYKKMKR KNVSLDEIYD ATAVRILVDT EAQCYEVLGM
VHTLWKQIPA EFDDYIINPK SNGYQSLHTA VEGPEGRVFE VQIRTFHMHD LAEMGVAAHW
KYKEGAVSQK ESHERKIEWL RDVLAWHQEM AANKGVAENV TTEFLEDRVY VFTPDGDVLD
LPHGVTPLDF AYHVHSNLGH RCRGAKVNGH IVPLTYQLKT GDRVEVLTGK EIKPSRDWIN
PHLNYLKTAR AKAKVLHWFK MQDYEDNVRD GRELLEKELK SLGIKSDKLN EVITALNYKK
ADDLYASLGR GDIKIGQIVN RLAPPDASEQ NLQKFVRQQQ KPEVTGSDLR IEGVGNLLTF
MARCCQPVPG DEIVGYITIG RGVSVHRKDC PNIIHASEKQ KRRFIQVNWG TATRENYVVD
VLIKAFDRSE LLKDVTSLLS NEKAHVYALQ THSNKHENMA YITLTVEIDG LNSLSRLLTK
LEQIPNVLEA RRQL
//
