ID I8R9N4_LACPE Unreviewed; 741 AA.
AC I8R9N4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA {ECO:0000313|EMBL:EIW13675.1};
GN ORFNames=KCA1_1701 {ECO:0000313|EMBL:EIW13675.1};
OS Lactiplantibacillus pentosus KCA1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW13675.1};
RN [1] {ECO:0000313|EMBL:EIW13675.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCA1 {ECO:0000313|EMBL:EIW13675.1};
RX PubMed=23527145;
RA Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA van Hijum S.A., Siezen R.J.;
RT "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT Healthy Premenopausal Woman.";
RL PLoS ONE 8:E59239-E59239(2013).
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:EIW13675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKAO01000043; EIW13675.1; -; Genomic_DNA.
DR AlphaFoldDB; I8R9N4; -.
DR PATRIC; fig|1136177.4.peg.1322; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000005826; 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; 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; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 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:EIW13675.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:EIW13675.1}.
FT DOMAIN 36..135
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 380..441
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT REGION 542..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 84750 MW; 7360C19EEC92FCEE CRC64;
MVQKYMNSDH VALVKRACDF ATYVHKDQYR QSGEPYIMHP IQVAGILAEL KMDPETVASG
FLHDVVEDTG VTLGDVEELF GHDVAVIVDG VTKLGKIRYK SNKEQLAENH RKLLLAMSKD
IRVMIVKLAD RLHNMRTLQH LRPDKQRRIA NETLEIYAPI ADRLGISTIK WELEDISLRY
LNPQQYYRIV HLMNSRREDR EKYIEIAIQD IQKALHDLEL PEAEIYGRPK HIYSIYKKMR
DKHKQFSQLY DLLAIRVVVD SIKDCYAVLG AIHTQWKPMP GRFKDYIAMP KANMYQSLHT
TVVGPEGKPL EIQIRTFEMH RVAEYGVAAH WAYKEGKRDE VQETQSGNKL NLVKEIIELQ
DESKDAADFM EGVKGDLFSD RVYAFTPKGD VTELPKGAGP LDMAYSIHTE VGNHTTGAKV
NGKIVPLDYQ IKNGDIVDIL TSTSSTGPSR DWQKLVYTRR ARNKIKQFFR NADREENIIS
GREMLEKQLR DLEFNPKEVM TKEKMTAVAQ KMHYSGEDDL FAALGFGDIQ PVGIANRLTS
DVRKEREATR QREREEAILA DSTESSTKKK SKDQQHEEQE KQERKRQKVS SSGGVIIQGV
DNLLVRLSHC CSPIPGDDIV GYITKGRGVS VHRVNCPNVK SAEANGERLI DVEWENPEGD
RTNYNSDLEI QGYNRNGMLN DVLKVINNHT KFLTNVNGKV DHNKMVIISV SLGVRNLEHL
QRIVDSLKNV QDVYVVERKM F
//
