ID A0A419T6S6_9FIRM Unreviewed; 758 AA.
AC A0A419T6S6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=BET01_15685 {ECO:0000313|EMBL:RKD33135.1};
OS Lacrimispora algidixylanolytica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD33135.1, ECO:0000313|Proteomes:UP000284277};
RN [1] {ECO:0000313|EMBL:RKD33135.1, ECO:0000313|Proteomes:UP000284277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPL73 {ECO:0000313|EMBL:RKD33135.1,
RC ECO:0000313|Proteomes:UP000284277};
RA Poppleton D.I., Gribaldo S.;
RT "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL Submitted (AUG-2016) 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:RKD33135.1}.
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DR EMBL; MCIA01000008; RKD33135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419T6S6; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000284277; Unassembled WGS sequence.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RKD33135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284277};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RKD33135.1}.
FT DOMAIN 67..167
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 684..758
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 758 AA; 86765 MW; 8EB7C10F5091D1B2 CRC64;
MAKREKQGLD TELEAPADFT SPEVLYEELV KSIRRYHPSD DITMIKKAYQ IAHDAHKDQK
RKSGEPYIIH PLCVAIILAD LEMDKETIAA GILHDVVEDT VMSLDELKSE FGEEVALLVD
GVTKLTQISW SMDKMELQAE NLRKMFLAMA KDIRVIIIKL SDRLHNMRTL QYMKPEKQKD
KARETMEIYA PIAHRLGISK IKIELDDLSL KYLHPDTYYE LAEKISLKKE TREYFVKSIV
DEVEEHLLTS GIEGKVDGRV KHFFSIYKKM VNQNKTLDQI YDLFAVRIIV ESVKDCYAAL
GVIHELYKPI PGRFKDYIAM PKPNMYQSLH TTLIGNNGQP FEIQIRTYEM HRTAEYGIAA
HWKYKESGSG QVAAAKEEEK LSWLRQILEW QKDMSDNMEF LNMVKGDLDL FSDSVYCFTP
SGDVKNLPSG STPIDFAYSI HSAVGNKMVG SRVNGKLVNI EYVIQNGDQV EIITSQNSRG
PSRDWLNIVK STQAKNKINQ WFKTELKEDN ILRGKEMVDK YCKTKGIVYS DINKPEYQDK
VMKRYAFRDW ESVIASIGHG GLKEGQVINK MIDEREKKLK KSVTDKTILN DIEDMSNKLP
VKRRSGSGIV VKGIHDLAVR FSKCCSPVPG DEIMGFVTRG RGISIHRTDC VNVLNLPEDE
RNRLIDAEWQ DQEGEATKER YSSEIKIFAN NRIGMFVDIS KVFTERQIDI TSMNSRTNKQ
GKATITMTFD IHGVEELGKL VDKLRQIEGV IDIERTAG
//
