ID S4AW18_ENTCA Unreviewed; 736 AA.
AC S4AW18;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=D932_02331 {ECO:0000313|EMBL:EPH62790.1};
OS Enterococcus casseliflavus 14-MB-W-14.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1259825 {ECO:0000313|EMBL:EPH62790.1, ECO:0000313|Proteomes:UP000014637};
RN [1] {ECO:0000313|EMBL:EPH62790.1, ECO:0000313|Proteomes:UP000014637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-MB-W-14 {ECO:0000313|EMBL:EPH62790.1,
RC ECO:0000313|Proteomes:UP000014637};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:EPH62790.1}.
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DR EMBL; ATIC01000025; EPH62790.1; -; Genomic_DNA.
DR RefSeq; WP_016609971.1; NZ_KE350230.1.
DR AlphaFoldDB; S4AW18; -.
DR PATRIC; fig|1259825.4.peg.2173; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000014637; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPH62790.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPH62790.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 662..736
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 736 AA; 84352 MW; DB0E3C6CECE1648D CRC64;
MAKEVILTGP NVIKLVAHYM SEEHVAFVQK ALDYATEAHK EQFRKSGEPY IIHPIQVAGI
LAELQMDPHT VATGFLHDVV EDTDVTLADL KEEFGADVAM LVDGVTKLGK IKYKSHEEQL
AENHRKMLIA MAQDLRVIMV KLADRLHNMR TLKHLREDKQ RRIAQETMEI YAPLAHRLGI
SRIKWELEDI SLRYLNPQQY YRIVHLMQTK REERESYVSE TVEEIRIATE ELDIYAEIYG
RPKHIYSIYR KMKDQKKQFN EIYDLLAIRV IVDSIKDCYA VLGTIHTKWK PMPGRFKDYI
AMPKANMYQS LHTTVIGPKG NPVEIQIRTH EMHEIAEFGV AAHWAYKEGK TEKVRADKMT
QQVGWFREIL ELQDESYDAS EFMEGVKGDI FSDKVYVFTP KGDVTELPQG SSPLDFAYSI
HTDIGNKTTG AKVNGKMVQL DYKLKNGDII EILTSPNSFG PSRDWVKLVA TSKAKNKIKR
FFKAQDRDEN IIKGHEAVVR TLQDMGFVPK EFLTKSKMAE ACERFNYQTE DDLFASVGYG
EVSPTTLANR LTEEERREKQ IEKQKQQVQE MINQPTKKEP EKMKVRHEGG IVIEGVDNLL
IRISRCCNPV PGDSIVGYIT KGRGISIHRS DCPNVQNKDA ANRLIDVEWE DATDINKEYD
ADLEIYGYDR CGLLNDGLQT GNTVTKRLVS VEAKTNKDKM ATIRITVAIQ NLTHLKSIVD
KIKQIPDVYS VRRTKG
//
