ID N2J3F5_9PSED Unreviewed; 747 AA.
AC N2J3F5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=HMPREF1487_07287 {ECO:0000313|EMBL:ENA31855.1};
OS Pseudomonas sp. HPB0071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA31855.1, ECO:0000313|Proteomes:UP000017050};
RN [1] {ECO:0000313|EMBL:ENA31855.1, ECO:0000313|Proteomes:UP000017050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPB0071 {ECO:0000313|EMBL:ENA31855.1,
RC ECO:0000313|Proteomes:UP000017050};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., Dai D.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., 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 Pseudomonas sp. HPB0071.";
RL Submitted (MAR-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 -!- 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:ENA31855.1}.
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DR EMBL; AQFP01000010; ENA31855.1; -; Genomic_DNA.
DR RefSeq; WP_010797458.1; NZ_KI517367.1.
DR AlphaFoldDB; N2J3F5; -.
DR GeneID; 84597749; -.
DR PATRIC; fig|1203578.3.peg.2990; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000017050; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017050}.
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 671..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 576..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 83828 MW; CA48FADD799288D1 CRC64;
MVQVRAHQPV NNDGSINIEA WLDHVQSMDP NFERQALLEA CEFARAAEAE AAPSEHLWAP
GTSSFQTGLE MAEILADLKL DQDSLVAALI YRAVREGKAS LEEAGKRFGP VVAKLIEGVL
RMAAISASLN PRQSMVLGTQ AQVDNLRRML VAMVDDVRVA LIKLSERTCA IRAVKNATDE
RRNRVAREVF DIYAPLAHRL GIGHIKWELE DLSFRYLEPI QYKQIATLLH ERRLDREQYI
ADVMQQLKQE LAATGVKADI SGRAKHIYSI WRKMQKKGLD FSQIYDVRAV RVLVPEIRDC
YTALGIVHTL WRHIPKEFDD YIANPKENGY RSLHTAVIGP EGKVLEVQIR THAMHEEAEL
GVCAHWRYKG TDVKSASSHY EEKISWLRQV LEWHEELGDI GGLAEQLRVD IEPDRVYVFT
PDGHAIDLPK GATPLDFAYR VHTEIGHNCR GAKINGRIVP LNYTLQTGEQ VEIITGKQGS
PSRDWLNPNL GYVMTSRARA KIVHWFKFQA RDQNVAAGKA MIDRELLRLA LPPVDYNTLA
EKVNYKNAED MQAALGAGDL RLAHVMHAAQ QLVEPEKETD PLDLLQRKPS PHKSGKRGDV
QINGVGNLLT QIAGCCQPVP GDPIVGYITL GRGVTIHRQD CQNALQLSSR EPERIIQVSW
GPVPVQTYPV DILVKAYDRP GLLRDVSQVL LNERINVLAV NTRSNKEENT ANMLLTIEIP
GLDALGRLLG RVSQLPNIIE ARRNRAT
//
