ID   RELA_STAAM              Reviewed;         736 AA.
AC   Q931Q4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=GTP pyrophosphokinase;
DE            EC=2.7.6.5;
DE   AltName: Full=(p)ppGpp synthase;
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
DE   AltName: Full=ppGpp synthase I;
GN   Name=relA; OrderedLocusNames=SAV1634;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       1/2.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB57796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000017; BAB57796.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q931Q4; -.
DR   SMR; Q931Q4; -.
DR   PaxDb; Q931Q4; -.
DR   EnsemblBacteria; BAB57796; BAB57796; SAV1634.
DR   KEGG; sav:SAV1634; -.
DR   HOGENOM; CLU_012300_3_0_9; -.
DR   OMA; DWISSPK; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.30.460.10; -; 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   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF19296; DUF5913; 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; SSF55021; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..736
FT                   /note="GTP pyrophosphokinase"
FT                   /id="PRO_0000166555"
FT   DOMAIN          57..156
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          400..461
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          662..736
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   736 AA;  84576 MW;  C158A507036972C1 CRC64;
     MNGVYHIMNN EYPYSADEVL HKAKSYLSAD EYEYVLKSYH IAYEAHKGQF RKNGLPYIMH
     PIQVAGILTE MRLDGPTIVA GFLHDVIEDT PYTFEDVKEM FNEEVARIVD GVTKLKKVKY
     RSKEEQQAEN HRKLFIAIAK DVRVILVKLA DRLHNMRTLK AMPREKQIRI SRETLEIYAP
     LAHHLGINTI KWELEDTALR YIDNVQYFRI VNLMKKKRSE REAYIETAID RIRTEMDRMN
     IEGDINGRPK HIYSIYRKMM KQKKQFDQIF DLLAIRVIVN SINDCYAILG LVHTLWKPMP
     GRFKDYIAMP KQNLYQSLHT TVVGPNGDPL EIQIRTFDMH EIAEHGVAAH WAYKEGKKVS
     EKDQTYQNKL NWLKELAEAD HTSSDAQEFM ETLKYDLQSD KVYAFTPASD VIELPYGAVP
     IDFAYAIHSE VGNKMIGAKV NGKIVPIDYI LQTGDIVEIR TSKHSYGPSR DWLKIVKSSS
     AKGKIKSFFK KQDRSSNIEK GRMMVEVEIK EQGFRVEDIL TEKNIQVVNE KYNFANEDDL
     FAAVGFGGVT SLQIVNKLTE RQRILDKQRA LNEEQEVTKS LPIKDNIITD SGVYVEGLEN
     VLIKLSKCCN PIPGDDIVGY ITKGHGIKVH RTDCPNIKNE TERLINVEWV KSKDATQKYQ
     VDLEVTAYDR NGLLNEVLQA VSSTAGNLIK VSGRSDIDKN AIINISVMVK NVNDVYRVVE
     KIKQLGDVYT VTRVWN