RELA_HAEIN
ID RELA_HAEIN Reviewed; 743 AA.
AC P44644;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=HI_0334;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
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DR EMBL; L42023; AAC21996.1; -; Genomic_DNA.
DR PIR; D64062; D64062.
DR RefSeq; NP_438498.1; NC_000907.1.
DR RefSeq; WP_005694339.1; NC_000907.1.
DR AlphaFoldDB; P44644; -.
DR SMR; P44644; -.
DR STRING; 71421.HI_0334; -.
DR EnsemblBacteria; AAC21996; AAC21996; HI_0334.
DR KEGG; hin:HI_0334; -.
DR PATRIC; fig|71421.8.peg.351; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OMA; TEIGHNC; -.
DR PhylomeDB; P44644; -.
DR BioCyc; HINF71421:G1GJ1-350-MON; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000000579; 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; IBA:GO_Central.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central.
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:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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; 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; 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..743
FT /note="GTP pyrophosphokinase"
FT /id="PRO_0000166549"
FT DOMAIN 58..161
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 404..465
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 670..743
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 743 AA; 84567 MW; 39B47619896AC211 CRC64;
MVAVRGSHLL NPQDFVIEQW CTGLKLAEQT EKSLIDAWYY ARDLMNAYPD EMKNATLMLQ
SGVEMVEILH ELNMDAETLL TAMLFPIVAN KLTDWESLKE KFGAKITKLL KGVLEMDNIR
QLNASHSANA LQVDNVRRML LAMVDDFRCV IIKLAERITF LRDAEHRCAE EDKVLAVKEC
SYIYAPLANR LGIGQLKWEL EDYCFRYLHP EQYRAIAKLL QERRLDREHY IADFVSELSG
YLRENIEQVE VYGRPKHIYS IWRKMQKKHL EFSGLYDVRA VRIIVQKLQD CYTALGIVHT
QFKHLPKEFD DYVANPKPNG YQSIHTVVLG KGGKPIEVQI RTQQMHDDAE LGMAAHWKYK
EGNTGSMSAY EEKIAWLRKL LAWQDDITDS GEVLAELRSQ VFDDRVYVFT PKGEVVDLPT
GSTPLDFAYA IHSEIGHRCI GAKVAGRIVP FTYQLQMGDQ IDIITQKNPN PSRDWLNPNL
GFTHTAKSRA KIQAWFKKQD RDKNIPAGKE LLDNELALLN LSIKQVEPYA LPRYNLKNLD
DLYAGIGSGD IRLNNLIHFL QSKLIKVTAE EADQEILRHV ANKSAVNSQQ KSEKNNGCVI
VEGVDNLMHH IARCCQPIPG DAIVGYITMG RGISIHRADC EQFLDLQAAH PERVVESIWG
ENYASGFHIN IRIVAGDRNG LLRDITTVLA NEKISVLGVS SRADTKKQLA TIDMEIELHN
VESLSKILAR LAKLDDVIEA KRL
