ID R5H994_9FIRM Unreviewed; 745 AA.
AC R5H994;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=BN469_01185 {ECO:0000313|EMBL:CCY26280.1};
OS Firmicutes bacterium CAG:114.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263001 {ECO:0000313|EMBL:CCY26280.1, ECO:0000313|Proteomes:UP000018090};
RN [1] {ECO:0000313|EMBL:CCY26280.1, ECO:0000313|Proteomes:UP000018090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:114 {ECO:0000313|Proteomes:UP000018090};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY26280.1}.
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DR EMBL; CAXW010000087; CCY26280.1; -; Genomic_DNA.
DR AlphaFoldDB; R5H994; -.
DR STRING; 1263001.BN469_01185; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000018090; 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:CCY26280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018090};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCY26280.1}.
FT DOMAIN 49..148
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 389..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..745
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 554..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 84572 MW; E0454D9837BF6E88 CRC64;
MEDKLEARFQ ELEEKLKNLT QEDRARVRDA FDYARSHHEG QLRKDGSPYI THPLEVAHLV
AELGLDADSI MAALLHDTIE DTDATHEEVA KRFSETVADL VEGVTKLTKV KYTSTEEKQM
ENLRKMLMAM AQDVRVILIK ICDRVHNIRT LEYQTEKKQR EKALETLEIY APIAHRLGMQ
RMKWEMEDQS LKFLDPIAYQ EISDELDRQA KAHAAFMEHI QEEITTRLEK EGIKGTVYGR
VKHVYSIYRK MYAQNKKLSE IFDLYAFRVI VDDIFTCYRV LGDIHDMYRP VLGRFKDYIS
TPKPNMYQSL HTTVIGSEGI PFEVQIRTWE MHHMAEYGVA AHWKYKQGMG NKKLGTEETF
AWVRRLLENQ QDTEAEEYIR TLKVDLFADE VFVFTPNADV INLPAGATPI DFAYAIHSAV
GNSMTGAKVN GRIVGFDYQL KSGEIVEVIT SKNAKGPSRD WMKLAKSNQA RTKIRQWFKR
EKREENVAHG RAMFEGEIKR LGLTIAMLTA EHMLPHILEK VRFNSLEEMY AAIGYGGASA
QKCANRAREE LVHQDRQQAE RLAAERAEKE AEEKAEAPSA LDAGVARAGN KKRSVSGVIV
SGMTECMVKF AKCCTPVPGD PIVGFITRGY GVSVHRSDCP NAVAGAQRPG EKDRWIKVSW
DPDSLNTYKT SLDLIAKDRP GLAMDVTTVM ATAKMNILGM TVNVLPDGYT KMNLVVEVRT
QSEVTTIMNK LNQVQGVYQV SRVSG
//
