ID R5CZY6_9FIRM Unreviewed; 749 AA.
AC R5CZY6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=BN705_01194 {ECO:0000313|EMBL:CCX72059.1};
OS Firmicutes bacterium CAG:555.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263030 {ECO:0000313|EMBL:CCX72059.1, ECO:0000313|Proteomes:UP000018402};
RN [1] {ECO:0000313|EMBL:CCX72059.1, ECO:0000313|Proteomes:UP000018402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:555 {ECO:0000313|Proteomes:UP000018402};
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:CCX72059.1}.
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DR EMBL; CAWW010000091; CCX72059.1; -; Genomic_DNA.
DR AlphaFoldDB; R5CZY6; -.
DR STRING; 1263030.BN705_01194; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000018402; 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:CCX72059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018402};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCX72059.1}.
FT DOMAIN 62..161
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..747
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 749 AA; 84592 MW; 14881D17A9B82493 CRC64;
MDADKSSVSL KRQPLDPDKM FAALEEKIKN SGVEMDMGRI RAAYDMARLA HSGQLRRDGS
PYVTHCVAAA DISVDMGLDE DSVVAALLHD VIEDTQLTHH DIARQFGEPV ANIVEGVTKL
TRVQYTSKED EQMENLRKML MAMAKDIRVI LIKIADRLHN MRTMAYQTEE KQRIKSLETM
EIYAPIAHRL GMQRAKWELE DLALMYLDPT GYNEIMQTLQ ERMPTLEAFT NDVEGQIKRR
LEEEGMHASV YSRIKHIYSI YRKMYAQKLD INGIFDLCAF RVIVDTIPDC YNVLGIIHDM
FKPVPGRFKD YISTPKPNMY QSVHTTVIGS QGIPFEVQIR TWEMHRTAEY GIAAHWKYKI
GDSGVKTGDE EKFAWVRRLL ESQQESDATD FFHNLKIDMF ADEVFVFSPK GDVINLPAGA
TPIDFAYSIH SAVGNSMVGA SVNGRIVTFD HVLQNGDIVE VRTAKNAPGP SRDWLNIAKS
GSARTKIKQW FKKERREENI ARGKEMFEAE LRNKGLRMDD ITGEDILPQL LKKVSYTSLD
EMYAAIGYGG MAATRAVNRI KDELARQQHA VDKRTVLDKV TEAAERREQM AKKAGKPVHG
ILVEGLDNCL IKFSRCCTPV PGDDIIGYIT RGQGVSIHRT DCENAKRRAE RPEDEGRWIN
VSWADEIHES YTTTLTVVSR ERGGLVMDIA TVMNALNTKV RSINARDTGD KSIVVITLET
KGLDELKSVI NRIQGVSGVV EVNRNGGKR
//
