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Database: UniProt
Entry: A0A2A5RLQ1_9LACT
LinkDB: A0A2A5RLQ1_9LACT
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ID   A0A2A5RLQ1_9LACT        Unreviewed;       741 AA.
AC   A0A2A5RLQ1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN   ORFNames=RT41_GL001504 {ECO:0000313|EMBL:PCS00193.1};
OS   Lactococcus fujiensis JCM 16395.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1291764 {ECO:0000313|EMBL:PCS00193.1, ECO:0000313|Proteomes:UP000218181};
RN   [1] {ECO:0000313|EMBL:PCS00193.1, ECO:0000313|Proteomes:UP000218181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16395 {ECO:0000313|EMBL:PCS00193.1,
RC   ECO:0000313|Proteomes:UP000218181};
RA   Sun Z., Zhong Z., Liu W., Zhang W., Zhang H.;
RT   "Draft genome sequences of 10 type strains of Lactococcus.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:PCS00193.1}.
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DR   EMBL; JXJU01000005; PCS00193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5RLQ1; -.
DR   STRING; 1291764.GCA_001311235_02339; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000218181; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; GTP PYROPHOSPHOKINASE; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000313|EMBL:PCS00193.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218181}.
FT   DOMAIN          51..150
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          395..456
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          666..741
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   741 AA;  84325 MW;  5A3FE70CEC5188A6 CRC64;
     MMPSEPILTG AQVVAMTEKY MNEKDVILVR RALDCAAIAH ADQYRASGEA YIVHPTQVAG
     ILAKLKLDAV TVACGFLHDV VEDTNFLSID LRELFGNEIA DIVEGVTKIG KVEYLSREKQ
     QAETHRKLLM AMSKDIRVIL VKLADRLHNM RTLKHLRPDK QKRISRETMD IYAPLADKLG
     IASIKWELED LSFRYLDEQE FYRIRGLMND KRANREQLVN EIISKLNERL ASAGVEGEEI
     YGRPKHIYSI YRKMHDKKKR FDEIYDLIAI RCITETTSDV YTTLGYIHDL WKPMPGRFKD
     YIANPKANGY QSVHTTVYGP KGPIEFQIRT REMHQIAEYG VAAHWAYKQG VKSKVNVHEI
     SETLNWIHEI VELREDAGDS AEDFVKAVQE DILSDKIYVF APDGAVQELP AGSGPIDFAY
     NIHTQVGDHA TGAKINGRMQ PLTYVLKTGD RVEIITSKSS FGPSRDWVNL VKTNKARNKI
     KQFFKNQDKE TSVNKGHELL LNALEDMGYV PNQYLDKKHL DDLFNKTSYR NIDALYAAIG
     FGEISATTIA NRLTEDERRR VERERQKVES EQLMNGEVKR EGKNVMKIRH DGGVSVSGID
     SLLVRIAKCC NPVPGDKIIG YITKGRGVSI HRDDCQNVRN QEDFDKRLVE VEWDDEDNNV
     KEYIANIDVY GFNRPGLLND VMQVLSNATK NLISINAQPT KDRKMANIHI AIGIKNLSEL
     TLIVDKIKMT PDVYSVKRTN A
//
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