ID A0A0R2B8B5_9LACO Unreviewed; 741 AA.
AC A0A0R2B8B5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=FC34_GL000425 {ECO:0000313|EMBL:KRM72715.1};
OS Lacticaseibacillus brantae DSM 23927.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423727 {ECO:0000313|EMBL:KRM72715.1, ECO:0000313|Proteomes:UP000051672};
RN [1] {ECO:0000313|EMBL:KRM72715.1, ECO:0000313|Proteomes:UP000051672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23927 {ECO:0000313|EMBL:KRM72715.1,
RC ECO:0000313|Proteomes:UP000051672};
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:KRM72715.1}.
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DR EMBL; AYZQ01000001; KRM72715.1; -; Genomic_DNA.
DR RefSeq; WP_057893734.1; NZ_AYZQ01000001.1.
DR AlphaFoldDB; A0A0R2B8B5; -.
DR STRING; 1423727.FC34_GL000425; -.
DR PATRIC; fig|1423727.3.peg.427; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000051672; 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:KRM72715.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000051672};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRM72715.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..741
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 741 AA; 84381 MW; E851918A2325AFE8 CRC64;
MAEEIELTQD DVMALCRQYM NDDHLAFVQK AYDFAAYVHH EQTRKSGEPY IIHPIQVAGI
LAELKMDPET VASGYLHDVV EDTNITLGDI QELFGNDVAV IVDGLTKLSK VTYVAHKDEL
AENHRKMLLA MAKDLRVIMV KLADRLHNMR TLMHLRPDKQ RRIANETLEI YAPLADRLGI
STIKWELEDL SLRYLNPQQY YRIAQLMNSK RAEREAYINA AIDDINRALD GLNMKYEIYG
RPKHIYSIYK KMRDKHKQFD ELYDLLAIRV ITESIKDCYA VLGAIHTKWK PMPGRFKDYI
AMPKANLYQS IHTTVIGPQG KPLEVQIRTE EMHHVAEYGV AAHWAYKEGQ TSEVQYDAAG
EKLDLFREIL EIQDESTDAA DFMESVKGDI FTDRVYVFTP KGDVYELPKG SGPLDFAYLV
HTEVGNHSVG AKVNGKIVPL NYQLKNGDIV DMLTSSQSTP SRDWMSVVYT SRARNKIRRY
FKQEDKEENT EKGRDMLERQ LTEMGLNPKT FMAKEPMADL LSRMNFQTED ELLSAIGYGE
YTALVVANRL TEKYRKQKAA EDQAAREKEI LDNNQKVTTM SKENQKPQTR TEDGVIIEGV
DNLLVHLAKC CLPVPGDAIV GYVTKGRGVT IHRADCPNVA NSAEMVGRLI DVRWENAGDS
SQLFNTDLEI YGYNRNGLLN DVLQALNAQT KSLNNVNGRV DHDKMADIHV TVGIRNLAHL
DKLMDAVKNI PDVYEVKREN G
//
