SPOT_HAEIN
ID SPOT_HAEIN Reviewed; 677 AA.
AC P43811;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase;
DE EC=3.1.7.2;
DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE Short=(ppGpp)ase;
GN Name=spoT; OrderedLocusNames=HI_1741;
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 degradation of ppGpp into GDP. It may also be
CC capable of catalyzing the synthesis of ppGpp (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC 1/1.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; L42023; AAC23388.1; -; Genomic_DNA.
DR PIR; F64139; F64139.
DR RefSeq; NP_439885.2; NC_000907.1.
DR AlphaFoldDB; P43811; -.
DR SMR; P43811; -.
DR STRING; 71421.HI_1741; -.
DR EnsemblBacteria; AAC23388; AAC23388; HI_1741.
DR KEGG; hin:HI_1741; -.
DR PATRIC; fig|71421.8.peg.1824; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OMA; DWISSPK; -.
DR PhylomeDB; P43811; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000000579; Chromosome.
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:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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; 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; 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; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 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 Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..677
FT /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT pyrophosphohydrolase"
FT /id="PRO_0000166571"
FT DOMAIN 18..117
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 360..421
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 601..675
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 677 AA; 76726 MW; FB12CE3C33A18B93 CRC64;
MIARDAHEGQ FRSSGEPYIT HPVAVASIIA QLHLDHEAVM AALLHDVIED TPYTEEQLKE
EFGASVAEIV DGVSKLDKLK FRTRQEAQVE NFRKMILAMT RDIRVVLIKL ADRTHNMRTL
GSLRPDKRRR IAKETLEIYC PLAHRLGIEH IKNELEDLSF QAMHPHRYEV LKKLVDVARS
NRQDLIERIS QEIKVRLENS GIFARVWGRE KHLYKIYQKM RIKDQEFHSI MDIYAFRVIV
KNVDDCYRVL GQMHNLYKPR PGRVKDYIAV PKANGYQSLQ TSMIGPKGVP VEVHIHTEDM
EQVAEMGITA HWVYKENGKN DSTTAQIRVQ RWLQSLVEIQ QSVGNSFEFI ENVKSEFFPK
EIYVFTPKGR IVELPMGATA VDFAYAVHSD VGNTCVGVTV EHKPYPLSKA LESGQTVNII
TDPNAHPEVA WLNFVVTARA KTRIRHYLKQ RCEEDAVKLG EVELNVALQP HNLGDFSIQQ
IRTVLDALAL SSLDELLREI GLGNQSASMI AHQFVGVPLE SANTKNLEFE SKILTIAPMQ
VGKTQFAQCC HPILGDPIVG CCTEKNTVVV HHQHCASLKN ACRQSLAKWD NVQSAVNFEA
ELQIEILNEQ NALLSLMTAI SASESSLQNI WTEELENNLL LVILQVCVKD IKHLANIVHR
IKGITGVVNV KRNINEL
