ID A0A0R2DI65_9LACO Unreviewed; 728 AA.
AC A0A0R2DI65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=FC86_GL000889 {ECO:0000313|EMBL:KRN03777.1};
OS Holzapfeliella floricola DSM 23037 = JCM 16512.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Holzapfeliella.
OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN03777.1, ECO:0000313|Proteomes:UP000051378};
RN [1] {ECO:0000313|EMBL:KRN03777.1, ECO:0000313|Proteomes:UP000051378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN03777.1,
RC ECO:0000313|Proteomes:UP000051378};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN03777.1}.
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DR EMBL; AYZL01000020; KRN03777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2DI65; -.
DR STRING; 1423744.FC86_GL000889; -.
DR PATRIC; fig|1423744.4.peg.914; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000051378; Unassembled WGS sequence.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRN03777.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000051378};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRN03777.1}.
FT DOMAIN 31..130
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 374..435
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 654..728
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 728 AA; 83451 MW; 4E5B507484C63311 CRC64;
MNQEHLDFVK KAYEFAAYLH KDQKRQSGQP YIIHPIQVAG SLAELRMDPE TIVSGFLHDV
VEDTEVTLGD VEELFGKDVA TIVDGVTKLG KIKYMSHEEQ LAENHRKMLI AMAQDLRVIM
VKLADRLHNM RTLGHLRPDK QRRISTETIE IYAPLADRLG ISKIKWELED ISLHYLNPQQ
YYRIVSLMKT KRSEREGYIA DAISTMETTL DDLNIEYNIY GRPKHIYSIY KKMKDKHKQF
DELYDLSAVR ILVKNVRDCY AVLGAVHTKW KPVPRRFKDY IAVPKANGYQ SLHTTIIGPG
GKPLEIQIRT EEMHEIAEFG IAAHWAYKEG VSSPVRIDEA GEKIDIFREI LDLREDSTNA
RDFMESVKGD LFSDRVYVFT PKGDVYELPK GSIPLDFAYL VHTEVGNHAV GARVNAKMVP
LDYKMKNGDI IEINTSSNAN PSRDWTNIVK TSRARNKIRR YFKNQTKDEN IEKGHNDIEN
QLIEMGYSPK EFMDKEHIQE LVDRFNFGSK EELFSSVGYG EITPLVAANR LTEKRRRENE
AQKRKELEDS ILSSVDNKAH NQIDRSKQHE PTKMQIQHEN GVIIQGLNNL LVRLAKCCNP
VPGDAIVGYV TKGRGVTIHR ADCSNISESD RIEGRVMDVE WMDVSSKDQT YFANLSIYGF
NRSGLLNDIL QKLNAVSKKL SNISGRVDHN DMAHVRLTVS VKNSQHLNEI LIQIKNIPDV
YEAKRADQ
//
