ID A0A0D0SF54_9FIRM Unreviewed; 742 AA.
AC A0A0D0SF54;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, 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=P261_00760 {ECO:0000313|EMBL:KIR01946.1};
OS Lachnospiraceae bacterium TWA4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR01946.1, ECO:0000313|Proteomes:UP000032079};
RN [1] {ECO:0000313|EMBL:KIR01946.1, ECO:0000313|Proteomes:UP000032079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR01946.1,
RC ECO:0000313|Proteomes:UP000032079};
RX PubMed=25495654;
RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT "Investigation of a new acetogen isolated from an enrichment of the tammar
RT wallaby forestomach.";
RL BMC Microbiol. 14:314-314(2014).
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:KIR01946.1}.
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DR EMBL; JPZU01000001; KIR01946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0SF54; -.
DR STRING; 1392836.P261_00760; -.
DR PATRIC; fig|1392836.3.peg.909; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000032079; 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:KIR01946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032079};
KW Transferase {ECO:0000313|EMBL:KIR01946.1}.
FT DOMAIN 51..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 397..458
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 668..742
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 742 AA; 84517 MW; FFFF283B861934F5 CRC64;
MEERTARELM QQLEQTIHKY HPSDDLSLVH KAYELADKAH EGQLRKSGEP YIIHPLHVAI
ILAELQLDKE SIVAGILHDV VEDTDYTRED IEQLFSSEVA LLVDGVTKLT QLSWSSDKIE
IQAENLRKMF LAMSKDIRVI LIKLADRLHN MRTLQFMKPS KQKEKARETM EIYAPIAQRL
GISKVKIELD DLALKYLEPE VYENLKESVA ACKGEREAFI NNITEEIRKY MEEAGYNDVL
VKGRAKHFFS IYKKMVNQHK TLEQIYDLFA VRIIVKDVKD CYGTLGIIHE KYKPIPGRFK
DYIAMPKSNG YQSLHTTLLS NDGRPFEIQI RTEDMHKTAE YGIAAHWKYK EGKAGENISA
REVDKMTWLR QILEYHQDLD NKEFMSTVKS DLDLFSDYVY CFTPTGDIKS LPAGSTPIDF
AYSIHSAVGN KMVGAKVNNR VVPIEYELKN GDQVAILTSQ NSKGPSRDWL KIVKSSQARN
KINQWFKTEF RADNILRGKE AVEKYCKSKG INFTEIFTQE GLEKVTKKYS YQNWDAILAA
IGHGGIKEGT VINKLQEIYN SSHEKKLTNE DILASITENS KVKQVLAKQG SGFIVNGTFD
PTARCSRCCN PLPGDEIVGF VTRGRGITVH RTDCSNILHL SDTEKARLTE VEWLVAEEVG
AVGNYSVTIN IYAFNRTQLL VDISKVFAEM DIDIEGINSH ISKQQIATLN ITFEINSVET
LNRLTKKLQQ IDGVQNIQRS RG
//
