ID A0A0W1A683_9GAMM Unreviewed; 734 AA.
AC A0A0W1A683;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KTD76859.1};
GN ORFNames=Lwor_2084 {ECO:0000313|EMBL:KTD76859.1};
OS Legionella worsleiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD76859.1, ECO:0000313|Proteomes:UP000054662};
RN [1] {ECO:0000313|EMBL:KTD76859.1, ECO:0000313|Proteomes:UP000054662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD76859.1,
RC ECO:0000313|Proteomes:UP000054662};
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; 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 -!- 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:KTD76859.1}.
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DR EMBL; LNZC01000027; KTD76859.1; -; Genomic_DNA.
DR RefSeq; WP_058493848.1; NZ_UGPA01000001.1.
DR AlphaFoldDB; A0A0W1A683; -.
DR STRING; 45076.Lwor_2084; -.
DR PATRIC; fig|45076.6.peg.2283; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000054662; Unassembled WGS sequence.
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:KTD76859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054662};
KW Transferase {ECO:0000313|EMBL:KTD76859.1}.
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; 83080 MW; 36EF5AFA6A324FE0 CRC64;
MVRVKDTTPL LPDGSIDVEQ WLHQLGSKGY LDNLELIRSA CSLSQLAGQD MGTETGQSCL
QQGLSMADLL ADLEVDHETL AAAIIFENVH YSDLSHEDVE EQLGHNIAKL VKGIEKMGAM
HNVQALNKYP QNKNQIDNIR KMLLAMVDDV RVVLIKLAER LCVLRSAGHL SEAVRKQLAT
EAMEIYAPLA NRLGIGAIKW EMEDLAFRYL HPEEYKSIAK GLKAKRLDRD NFVNMIVEEL
NTHIRATGAH HFAVYGRSKH IHSIYKKMQR KNVSLEEIYD ATAVRILVDT EAQCYEVLGM
VHTLWKQIPA EFDDYIFHPK QNGYQSLHTA VEGPEGRVFE VQIRTFHMHD LAEMGVAAHW
KYKEGGVSHK ESHERKIEWL RDVLAWHQEM AANKGVAENI STEFLEDRVY VFTPDGDVLD
LQQGVTPLDF AYHVHSDLGH RCRGAKINGH IVPLTYQLKT GDKVEVLTGK EIKPSRDWIN
PHLNYLKTAR AKAKVLHWFK MQDYDNNVQD GRELLDKELK SLGIKSDKLN EVAVALNYKK
VDDLYACLGR GDIKISQIVN RLAPPETSEH SAIKLAKPQQ MPEITGSDLR IEGVGNLLTF
MARCCQPVPG DEVIGYITIG RGVSIHRKDC PNILHASEKQ KQRFLQVNWG ASTRENYIVD
VLIKAFDRSE LLKDVTSLLS NEKAHVYSLQ TSTDKHENMA YITLTVEIDG LSSLSRLLAK
LEQIPNVLEA RRQV
//
