ID A0A433SGL0_9BURK Unreviewed; 751 AA.
AC A0A433SGL0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:RUS67889.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:RUS67889.1};
GN Name=relA {ECO:0000313|EMBL:RUS67889.1};
GN ORFNames=CUZ56_00370 {ECO:0000313|EMBL:RUS67889.1};
OS Saezia sanguinis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Saezia.
OX NCBI_TaxID=1965230 {ECO:0000313|EMBL:RUS67889.1, ECO:0000313|Proteomes:UP000286947};
RN [1] {ECO:0000313|EMBL:RUS67889.1, ECO:0000313|Proteomes:UP000286947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNM695-12 {ECO:0000313|EMBL:RUS67889.1,
RC ECO:0000313|Proteomes:UP000286947};
RA Medina-Pascual M.J., Valdezate S., Monzon S., Cuesta I., Carrasco G.,
RA Villalon P., Saez-Nieto J.A.;
RT "Saezia sanguinis gen. nov., sp. nov., in the order Burkholderiales
RT isolated from human blood.";
RL Submitted (JAN-2018) 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 -!- 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:RUS67889.1}.
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DR EMBL; PQSP01000001; RUS67889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433SGL0; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000286947; 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:0016779; F:nucleotidyltransferase 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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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:RUS67889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000286947};
KW Transferase {ECO:0000313|EMBL:RUS67889.1}.
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 675..751
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 751 AA; 84247 MW; 20F7797E57A699F4 CRC64;
MKTNTISSDA VSLIQLKDGE NVRETLADAV DRPDVARARA FVEPLINGFA LSTGEDTLAH
ADAVVQILKE LDGSESLQTA AYLVYAIEHI QRPKEVIEKA FGSSMANLVI DTHRLIQVQH
SARQNAVVND NDAMAQTERA RKMLLAFSRD LRGVMLRLAS RLQTMRYCAT HRVELPKSMA
EETLNVFAPL ASRLGIWQIK WELEDLAFRF IQPETYQQIA KLLDEPRIER ENYIAHVEKY
LINSLRELGI DAKVTGRPKH IYSIWKKMHG KSLDFDQVYD LRAFRIIVPS VQDCYTVLAW
INAHFEQIPS EFDDYIAKPK VNGYQSLHTV VKDTSEAGRG KCLEIQIRTQ DMHDRAENGV
AAHWAYKEAG SKGYSGVVAN SDYDARIAML RQLLAWERDL SHHATEEGAS LFDDRIYVLT
PMATFIELPQ GSTPLDFAYA VHTDLGHKCR GAKVDGMMVP LDTPLQNGQT VEIVSAKEGG
PSRDWLNSDE HYLASPRAKA KVRAWFNAQV TQQTIARGRE QVEKLLQREG KTALKLDDLA
AKLGFKNADS LFEVIGKDEY SLRNIEQIFK PVVQESPQEA LLSASRKPQP ASSHKGGVLV
VGMDSLLTQL AKCCKPAPPD AIVGYVTRGK GVSIHRSDCT NIKELEQREP ERVIEVQWEA
PQASENGHLP VYPVDIEVWA VDRQGLLRDI SEVLSKEHIN VIGVNTQSLR HRLHGDSAWM
TFTVEVADTE RLKRALNQVS AVSGVRSANR R
//
