ID A0A1W1UER1_9PAST Unreviewed; 740 AA.
AC A0A1W1UER1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=SAMN05660772_00413 {ECO:0000313|EMBL:SMB79550.1};
OS Pasteurella testudinis DSM 23072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1122938 {ECO:0000313|EMBL:SMB79550.1, ECO:0000313|Proteomes:UP000192408};
RN [1] {ECO:0000313|EMBL:SMB79550.1, ECO:0000313|Proteomes:UP000192408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23072 {ECO:0000313|EMBL:SMB79550.1,
RC ECO:0000313|Proteomes:UP000192408};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWWV01000002; SMB79550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1UER1; -.
DR STRING; 1122938.SAMN05660772_00413; -.
DR Proteomes; UP000192408; 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:SMB79550.1};
KW Transferase {ECO:0000313|EMBL:SMB79550.1}.
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 665..740
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 740 AA; 84577 MW; 5F8106A565CB9425 CRC64;
MVAIRASHLL TPAQFVVEDW SERLPLAPAV RQTLIETWHY NDAKLQNLET KERQYLLYAA
SEMVEVLSGL NMDQDSLLAA MLFPLVRRRV LNYEQIKEDF GNDIRKLVKG VVDMDGIRQL
SASQSGSHLQ VDNVRRMLLA MVDDFRCVVI KLAERVAFLR EENNFISEPE KILAARECSN
IYAPLANRLG IGQLKWELED YCFRYLDPDN YRKIAKLLHE KRRDREAYIH DFVAVIERDL
QAELPVAAQV YGRPKHIYSI WKKMQKKNLP FEQLFDIRAV RIIVDKLEDC YTALGIVHSH
FKHIAAEFDD YVAHPKPNGY QSIHTVVLGE GGKAIEVQIR TQQMHDNAEL GVAAHWKYKE
GSTGGRAGYE QKITWLRQVL AWQHDLSQSG DVMEETRSKI FDDRIYVFTP QGDIVDLPVG
STPLDFAYTI HSEVGHRCVG AKVADKIVPF TYKLQMGDKV EILTQKNPNP SRDWLNPNTG
FVTINRVRSK IQAWFKRQDR EKNIPLGKEL LEAEMAKLGL NYKQIEEYAL PRHNLKQLED
LYAGIGNGDI RLNQLSNYLQ GKLLRPTAEE VDEHILRQVE NKQQHKASSN KGQIVIEGVG
NLMHHIARCC QPIPGDHILG YITQGRGISI HRADCEQVLN LQEACPERVV EAIWGESYHT
KFNLVIRVVA NDRTGLLRDI TTVLANEKVS VLRVSSKSDV KNMTATIDME IELGNVSMLA
RILSSLLRIN DVVEARRLSS
//
