ID K9DKV6_9FIRM Unreviewed; 744 AA.
AC K9DKV6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=HMPREF9282_00220 {ECO:0000313|EMBL:EKU79412.1};
OS Veillonella seminalis ACS-216-V-Col6b.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=883156 {ECO:0000313|EMBL:EKU79412.1, ECO:0000313|Proteomes:UP000009891};
RN [1] {ECO:0000313|EMBL:EKU79412.1, ECO:0000313|Proteomes:UP000009891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-216-V-Col6b {ECO:0000313|EMBL:EKU79412.1,
RC ECO:0000313|Proteomes:UP000009891};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Veillonella ratti ACS-216-V-COL6B.";
RL Submitted (SEP-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:EKU79412.1}.
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DR EMBL; AHAF01000001; EKU79412.1; -; Genomic_DNA.
DR AlphaFoldDB; K9DKV6; -.
DR STRING; 883156.HMPREF9282_00220; -.
DR PATRIC; fig|883156.3.peg.221; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000009891; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 63..162
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 668..742
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 744 AA; 85166 MW; 84A4487F4D399C2E CRC64;
MAENEEGKVI VDQPVFNKEV ELAHLMEIVR SYLDEADCKE IMRAFEVADK AHAPQKRASG
EPYILHPLAV ATILANLQID ATTVIAALLH DVVEDTEYTL PQIEELFGKE VAFLVDGVTK
LNQFQYHTKE DQQLENYRKM ILAMAKDVRV VVIKLGDRLH NMRTLKHMRS DKQKRIAQET
LEIFAPLAHR LGIFNIKWEL EDLSFRYLEP DKYYDLVEQM QEKRHVREEI VNDTMEQLKK
ALEDAHIKAD VKGRPKHFYS IYKKMKKDNR DLSQIYDLYA VRVIVDTIPD CYAVLGIVHN
LWKPLPYRFK DYIAMPKSNM YQSLHTTIIG TMGHSVEIQI RTWEMHRVSE YGVAAHWRYK
EGNKGGDKDF DQKVGWLRQV LEWQDASNPK ELVNALKLDV FSGEVFVFTP RGDVLKLPKG
AVPLDFAYRI HTDVGHHCVG AKVNGKIVSL DYTLQNGDIV DIITSKTGKP SLDWLNIVGS
TESRSKIRNW FKKENKEENI VKGRELLEKE AKRLNYEWKE LNKPGRMEQI AKALNAGSET
ELLSAVGYGG IPVNSVLLRF VDLYKRDLAK EDNRRDTMAL LEKLKTPERV HRKSSTGILV
NGEPDVMVRM ARCCNPVPGD EVVGYITRGR GVSVHRADCP NIGHTPEDVD RMIEVSWDAG
TSENFHVAIE ITAYDRGGLL MEIMATLSEM KINIVNINAK VDDTKNANIN LVIEIRDVSE
LDFVMTKVRR IRDVYTVQRA NGGS
//
