ID W1Q5D4_ABIDE Unreviewed; 736 AA.
AC W1Q5D4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=GCWU000182_000158 {ECO:0000313|EMBL:ESK66470.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK66470.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK66470.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK66470.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., 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:ESK66470.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACIN03000001; ESK66470.1; -; Genomic_DNA.
DR RefSeq; WP_023390818.1; NZ_KI535340.1.
DR AlphaFoldDB; W1Q5D4; -.
DR STRING; 592010.GCWU000182_000158; -.
DR GeneID; 84816324; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000019050; 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:ESK66470.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000019050};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ESK66470.1}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..735
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 736 AA; 83767 MW; 2EDA26515A73F0AA CRC64;
MAQAPDLTAA DVMALCESYM NEKHVAFVKK ALDFATEAHK EQFRLSGEAY IVHPIQVAGI
LAQLKMDPDT VATGFLHDVV EDTDYTLEDI VHEFSETVAF LVDGVTKLGK FKFQSKEEAL
AENHRKMLLA MAKDMRIIMV KLADRLHNMR TLKFQKPAKQ VEKSQEAIEI YAPLADRLGM
NLIKWELEDI ALRYTNPDAY YQIVNLMKSK REERETYIQE AIKDINEAIE ELHIKADVYG
RPKHIYSIYR KMVKQNKDFD EIYDLLAIRA LVPTIKDCYA VLGAVHTKWK PMPGRFKDYI
AMPKANLYQS IHTTVIGPHG KPVEIQIRTF QMNEVAEYGV AAHWAYKEGK TQQVREDEAI
KKQLTWFRDI VELEDEAKDA GEFMDFVKED IFKDQVYVFS PKGDVFELPN GAGPLDFAYH
VHTDVGQKTI GAKVNGKIVP LNYKLKNGDI VDILTNPNSN GPSRDWLKYT ATSKARNKIK
RYFKLLDRDR NSERGQAMVE EELKKNGYSL KQLAKKAYEK ELFERYNVPT LADLFAAVAL
GEVSAISVYN FLHSKEQKDV PPAEPLTNEQ TLNKPETEAM KIQHENGVMV RGVNNLMIRL
SRCCSPVPGD QIVGYVTRGR GISVHRKDCP NLLNEPDLQQ RTIPVEWEST GQLGADYVTE
IRVVGFDRNG LINEVLHVVN HSVKTLRNVN GKVDDKTSTA TVTIKVAISN TAQLEDLMVK
LRSIPDVYEV TRVNNK
//
