ID Q2FXU1_STAA8 Unreviewed; 729 AA.
AC Q2FXU1;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, 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 OrderedLocusNames=SAOUHSC_01742 {ECO:0000313|EMBL:ABD30813.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30813.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL (2006).
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 This enzyme catalyzes the formation of pppGpp which is then hydrolyzed
CC to form ppGpp. {ECO:0000256|ARBA:ARBA00024961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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; CP000253; ABD30813.1; -; Genomic_DNA.
DR RefSeq; WP_001058583.1; NZ_LS483365.1.
DR RefSeq; YP_500249.1; NC_007795.1.
DR AlphaFoldDB; Q2FXU1; -.
DR SMR; Q2FXU1; -.
DR STRING; 93061.SAOUHSC_01742; -.
DR PaxDb; 1280-SAXN108_1661; -.
DR GeneID; 3920542; -.
DR KEGG; sao:SAOUHSC_01742; -.
DR PATRIC; fig|93061.5.peg.1587; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
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: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; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 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; PS51831; HD; 1.
DR PROSITE; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000313|EMBL:ABD30813.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 655..729
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 729 AA; 83694 MW; 34ACEC782996C6BC CRC64;
MNNEYPYSAD EVLHKAKSYL SADEYEYVLK SYHIAYEAHK GQFRKNGLPY IMHPIQVAGI
LTEMRLDGPT IVAGFLHDVI EDTPYTFEDV KEMFNEEVAR IVDGVTKLKK VKYRSKEEQQ
AENHRKLFIA IAKDVRVILV KLADRLHNMR TLKAMPREKQ IRISRETLEI YAPLAHRLGI
NTIKWELEDT ALRYIDNVQY FRIVNLMKKK RSEREAYIET AIDRIRTEMD RMNIEGDING
RPKHIYSIYR KMMKQKKQFD QIFDLLAIRV IVNSINDCYA ILGLVHTLWK PMPGRFKDYI
AMPKQNLYQS LHTTVVGPNG DPLEIQIRTF DMHEIAEHGV AAHWAYKEGK KVSEKDQTYQ
NKLNWLKELA EADHTSSDAQ EFMETLKYDL QSDKVYAFTP ASDVIELPYG AVPIDFAYAI
HSEVGNKMIG AKVNGKIVPI DYILQTGDIV EIRTSKHSYG PSRDWLKIVK SSSAKGKIKS
FFKKQDRSSN IEKGRMMVEA EIKEQGFRVE DILTEKNIQV VNEKYNFANE DDLFAAVGFG
GVTSLQIVNK LTERQRILDK QRALNEAQEV TKSLPIKDNI ITDSGVYVEG LENVLIKLSK
CCNPIPGDDI VGYITKGHGI KVHRTDCPNI KNETERLINV EWVKSKDATQ KYQVDLEVTA
YDRNGLLNEV LQAVSSTAGN LIKVSGRSDI DKNAIINISV MVKNVNDVYR VVEKIKQLGD
VYTVTRVWN
//