ID Q7TUG7_PROMP Unreviewed; 769 AA.
AC Q7TUG7;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-diphosphatase, (PpGpp)ase {ECO:0000313|EMBL:CAE18650.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:CAE18650.1};
GN Name=spoT {ECO:0000313|EMBL:CAE18650.1};
GN OrderedLocusNames=PMM0191 {ECO:0000313|EMBL:CAE18650.1};
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE18650.1, ECO:0000313|Proteomes:UP000001026};
RN [1] {ECO:0000313|EMBL:CAE18650.1, ECO:0000313|Proteomes:UP000001026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4
RC {ECO:0000313|Proteomes:UP000001026};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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 {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; BX548174; CAE18650.1; -; Genomic_DNA.
DR RefSeq; WP_011131830.1; NC_005072.1.
DR AlphaFoldDB; Q7TUG7; -.
DR STRING; 59919.PMM0191; -.
DR KEGG; pmm:PMM0191; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_3; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000001026; Chromosome.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CAE18650.1}.
FT DOMAIN 85..184
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 426..488
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 694..768
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 769 AA; 87011 MW; 0AA58C374DC6296B CRC64;
MAEATANSKE KNEIKVSTII LPENKNYESE SLKYEINIPN WLLEIIQNYE VSNKKNNSNQ
DLIVKAFKLA YEAHNGQLRA SGEPYIIHPL AVADLLKEIG ASSSVVAAGL LHDVVEDTGI
ALSEIEVNFG LEVKVLVEGV TKLGGIHFNN RTEAQAENLR KMFLAMASDI RVVLVKLADR
LHNMRTIQWL NEERKERIAR ETREIYAPLA NRLGINRFKW ELEDLAFKFL EPEEYKNLKD
QIAVKRSDRE KRLNVTLNLM KENLVSSGLV NFEITGRPKH LYGIWSKMER QQKQFGEIYD
VAALRIIVSN TDSCYKALAV VHDTFRPIPG RFKDYIGLPK PNGYQSLHTS VIGRHRPIEV
QIRTSSMHQI AEFGIAAHWQ YKEGGSPASS NAERFNWLRQ LVEWQQEGNE KDHNDYLASI
KEDLFDEEVF VITPKGDVVG LRKGSTAIDF AYRIHSEIGN HCNGIRINEK LSPLSTSLQN
GDFIEILTNT NSTPSLDWLN FVVTPTAKNR IRQWYKKSHR DETIKRGKDL LEKEIGRNGF
ESLISSDAMK KVAHRCNLKS TEDLLASLGF GGLTLHQVLN RLREEIKIQT EEIKNESNEE
LARSLINKNN SIATKSHATN KSPITGVEGL DYRIGKCCSP LPGEEIIGTV SLGNHGITIH
RRDCENVIPI PIERRLPVAW NQENKILDNK FPIQLRIEVI DRVGVLKDIL MRLSDKGINV
SDANVKTAFG KPAIINLCVG LESYSQLHKT IDQIKSMADV LDIARVGIS
//
