RELA_STAEQ
ID RELA_STAEQ Reviewed; 729 AA.
AC Q5HNR8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SERP1196;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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 ---------------------------------------------------------------------------
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; CP000029; AAW54575.1; -; Genomic_DNA.
DR RefSeq; WP_001832683.1; NC_002976.3.
DR AlphaFoldDB; Q5HNR8; -.
DR SMR; Q5HNR8; -.
DR STRING; 176279.SERP1196; -.
DR PRIDE; Q5HNR8; -.
DR EnsemblBacteria; AAW54575; AAW54575; SERP1196.
DR GeneID; 50018568; -.
DR KEGG; ser:SERP1196; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OMA; DWISSPK; -.
DR OrthoDB; 204079at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000000531; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..729
FT /note="GTP pyrophosphokinase"
FT /id="PRO_0000166562"
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 655..729
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 729 AA; 83468 MW; 2EEE5C9BEF92E0DA CRC64;
MNNEYPYSAD EVLYKAKSYL STSEYEYVLK SYHIAYEAHK GQFRKNGLPY IMHPIQVAGI
LTEMRLDGPT IVAGFLHDVI EDTSYTFEDV KDMFNEEIAR IVDGVTKLKK VKYRSKEEQQ
AENHRKLFIA IAKDVRVILV KLADRLHNMR TLKAMPREKQ VRISKETLEI YAPLAHRLGI
NTIKWELEDT ALRYIDSVQY FRIVNLMKKK RSEREAYITN AINKIKNEMT KMNLSGEING
RPKHIYSIYR KMIKQKKQFD QIFDLLAIRI IVNSINDCYA TLGLVHTLWK PMPGRFKDYI
AMPKQNMYQS LHTTVVGPNG DPLEIQIRTH EMHEIAEHGV AAHWAYKEGK TVNQKTQDFQ
NKLNWLKELA ETDHTSADAQ EFMESLKYDL QSDKVYAFTP ASDVIELPYG AVPIDFAYAI
HSEVGNKMIG AKVNGKIVPI DYVLQTGDII EIRTSKHSYG PSRDWLKIVK SSSAKSKIKS
FFKKQDRSSN IEKGKFMVEA EIKEQGFRVE DILTEKNLEV VNEKYHFAND EDLYAAVGFG
GVTSIQIVNK LTERQRILDK QKALNEAQEV TKSVPIKKDI TTDSGVYVEG LENVLIKLSK
CCNPIPGDDI VGYITKGHGI KVHRTDCPNI KNETDRLISV EWVKSKDSTQ QYQVDLEVTA
YDRNGLLNEV LQAVNSTAGS LIKVSGRSDI DKNAVINISV MVKNVNDVYR VVEKIKQLGD
VYTVSRVWN