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 27-MAR-2024, entry version 131. 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; Bacillota; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000017; BAB57796.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_001058580.1; NC_002758.2. DR PDB; 7OIW; X-ray; 2.63 A; A/B=1-438. DR PDBsum; 7OIW; -. DR AlphaFoldDB; Q931Q4; -. DR SMR; Q931Q4; -. DR KEGG; sav:SAV1634; -. DR HOGENOM; CLU_012300_3_0_9; -. 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; 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; PS51880; TGS; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; GTP-binding; Kinase; Nucleotide-binding; KW 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" FT HELIX 16..24 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 29..45 FT /evidence="ECO:0007829|PDB:7OIW" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 75..83 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 103..114 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 142..157 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 164..176 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 178..184 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 188..202 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 204..239 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 243..249 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 252..260 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 272..281 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 282..295 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:7OIW" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 318..323 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:7OIW" FT STRAND 329..336 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 337..345 FT /evidence="ECO:0007829|PDB:7OIW" FT HELIX 346..350 FT /evidence="ECO:0007829|PDB:7OIW" 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 //