ID A0A0W0ZVK5_9GAMM Unreviewed; 734 AA.
AC A0A0W0ZVK5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
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:KTD73197.1};
GN ORFNames=Ltuc_1044 {ECO:0000313|EMBL:KTD73197.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD73197.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD73197.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD73197.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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. {ECO:0000256|ARBA:ARBA00025704}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD73197.1}.
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DR EMBL; LNZA01000001; KTD73197.1; -; Genomic_DNA.
DR RefSeq; WP_058520257.1; NZ_LNZA01000001.1.
DR AlphaFoldDB; A0A0W0ZVK5; -.
DR STRING; 40335.Ltuc_1044; -.
DR PATRIC; fig|40335.7.peg.1098; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000054693; Unassembled WGS sequence.
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; 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:SF31; 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; 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:KTD73197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693};
KW Transferase {ECO:0000313|EMBL:KTD73197.1}.
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; 83051 MW; 61A465387B30BCE2 CRC64;
MVRVKDTIPL CEDGSIDVDL WLHQLGAKGY LNNLELIRSA CTLSQLAGQE HATETGQSCL
QQGLSMADLL ADLEVDQETL AAAIIFENVH YADLSIDDVV EQLGPNIAKL VKGIERMSAM
HSFQGLNKYP QNKQQIDNLR KMLLAMVDDV RVVLIKLAER LCVLRTAGHL SEELRKQLAT
EAMEIYAPLA NRLGIGAIKW EMEDLAFRHM HPEDYKAIAK GLKAKRLERD NFVNAIVAQL
NEQIKASGID HFAVYGRSKH IHSIYKKMTR KNVSLDEIYD ATAVRVLVNT QPQCYEVLGM
VHTLWKQIPA EFDDYIINPK PNGYQSLHTA VKGPEGRVFE VQIRTFHMHD LAEMGVAAHW
KYKEGGFKQK QSHERKIEWL RDVLAWHREM ASNKGVPEST TTEFLEDRVY VFTPDGDVLD
LPHGVTPLDF AYHVHSDLGH RCRGARINGH IAPLTYQLKT GDRVEILAGK ESKPSRDWIN
PHLNYLKTSR AKAKVLHWFK MQDYDRNIQD GRELLDKELK SLGIKSDKLN EAAAALHFKK
LDDLYANLGR GDIKIGQIIS KLTPPTTSEL NLERFVRPQA KPEITGSDLR IEGVGNLLTF
MARCCQPVPG DPVIGYITIG RGVSVHRQDC PNIIHANERQ KQRFLQVTWG SATRENYVVD
ILIKAFDRSE LLKDVTSLLA NEKAHVYALQ TQSNKQENMA YITLTVDVDG LSSLSRLLTK
LEQIPNVLEA RRQV
//