ID E6LDR3_ENTI1 Unreviewed; 745 AA.
AC E6LDR3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA2 {ECO:0000313|EMBL:EFU74652.1};
GN ORFNames=HMPREF9088_0503 {ECO:0000313|EMBL:EFU74652.1};
OS Enterococcus italicus (strain DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=888064 {ECO:0000313|EMBL:EFU74652.1, ECO:0000313|Proteomes:UP000010296};
RN [1] {ECO:0000313|EMBL:EFU74652.1, ECO:0000313|Proteomes:UP000010296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15952 / CCUG 50447 / LMG 22039 / TP 1.5
RC {ECO:0000313|Proteomes:UP000010296};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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:EFU74652.1}.
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DR EMBL; AEPV01000018; EFU74652.1; -; Genomic_DNA.
DR AlphaFoldDB; E6LDR3; -.
DR STRING; 888064.HMPREF9088_0503; -.
DR PATRIC; fig|888064.11.peg.454; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000010296; 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:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000010296};
KW Transferase {ECO:0000313|EMBL:EFU74652.1}.
FT DOMAIN 58..157
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 401..462
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..745
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 745 AA; 84973 MW; CA5BEAACF8FF5DE7 CRC64;
MFKEGVGSMA KDIILTGPGV INMVARYMSA EHVAFVQKAL DYATSAHEGQ FRKSGEPYII
HPIQVAGILA ELQMDPHTVA TGFLHDVVED TDVTLQDLTE EFGPDVAMLV DGVTKLGKIK
YKSHEEQLAE NHRKMLIAMA QDLRVIMVKL ADRLHNMRTL KHLREDKQRR IARETLDIYA
PLAHRLGISR IKWELEDRSL RYINPQQYYR IVHLMKTKRD EREAYVDKTV EELRIATEEL
DIYAEIYGRP KHIYSIYRKM VDKKKQFDEI YDLLAIRVIV DSIKDCYAVL GTIHTKWKPM
PGRFKDYIAM PKANMYQSLH TTVIGPNGNP VEIQIRTHEM HEIAEFGVAA HWAYKEGKTD
KVNPDQMTEQ VGWFKEILEL KDESYDASDF MEGVKGDIFS DKVYVFTPNG DVSELPQGSS
PLDFAYNIHT DIGNKTVGAK INGKMVQLDY KLKNGDIVEI MTSPNSFGPS RDWLKLVATS
KAKNKIKRFF KTQDRDANVV KGHDAVVRTL TEMGFVPKEI LTKTKLQEAL GRFNYQTDED
LFAAVGFGEV SPTTLANRLT EEERKERDIE KQKQQVQDLL NQPVKKEPEK MKVRHEGGIV
IQGVDNLLVR ISRCCNPVPG DPIVGYITKG RGISIHRADC PNVHSSEDVE ERLIEVEWED
TASKEKEYDA DIEIYGYDRS GLLNDILQTV SSMSKRLVGV EARSNKEKTA TIRLTVGIQN
LAHLHSIVEK IKQVPDVYSV RRMKG
//
