ID E6KZU7_9PAST Unreviewed; 742 AA.
AC E6KZU7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
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 Name=relA {ECO:0000313|EMBL:EFU67044.1};
GN ORFNames=HMPREF9064_1679 {ECO:0000313|EMBL:EFU67044.1};
OS Aggregatibacter segnis ATCC 33393.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU67044.1, ECO:0000313|Proteomes:UP000032871};
RN [1] {ECO:0000313|EMBL:EFU67044.1, ECO:0000313|Proteomes:UP000032871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU67044.1,
RC ECO:0000313|Proteomes:UP000032871};
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 -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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:EFU67044.1}.
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DR EMBL; AEPS01000011; EFU67044.1; -; Genomic_DNA.
DR RefSeq; WP_006719486.1; NZ_LS483443.1.
DR AlphaFoldDB; E6KZU7; -.
DR STRING; 739.GCA_001059425_00932; -.
DR GeneID; 60799123; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000032871; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EFU67044.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032871};
KW Transferase {ECO:0000313|EMBL:EFU67044.1}.
FT DOMAIN 58..161
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 404..465
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 669..742
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 742 AA; 84624 MW; 0D4B4040A96E3282 CRC64;
MVAVRGSHLL NPKDFEIEKW CANLNVAENV KANLITAWHY SQQKMTLRAE HQQEEAHLLT
FGVEMVEILN SLNMDADSLF TAMLFPIVRD QLVDLAQIEE DFGANISKLV RGVIEMDNIR
QLNITHSASS LQVDNVRRML LAMVDDFRCV IIKLAERIAF LRDAEKNYTE EERVLAAKEC
ANIYAPLANR LGIGQLKWEL EDYCFRYLHP EQYRAIAKLL KERRLDREQY IADFVSELSG
YLQENIPQVE VYGRPKHIYS IWRKMQKKHL EFSDLYDVRA VRIVVQKLQD CYTALGIVHT
HFKHLPKEFD DYVANPKPNG YQSIHTVVLG KGGKPIEVQI RTQQMHDDAE LGVAAHWKYK
EGASAGRNGY EEKIAWLRKL LAWQDDIADS GEVMAELRSQ VFDDRVYVFT PKGEVVDLPT
GSTPLDFAYA IHSEIGHRCI GAKVGGRIVP FTYQLQMGDQ VDIITQKNPN PSRDWLNPNL
GFTHTAKARA KIHAWFKKQD RDKNIPAGKE LLESEINRLG ISLKQVEQQA LPRYNLKNLD
DLYAGIGGGD IRIGPLINFL QNKFIKISAQ EVDEEILRHV STKSAANAQQ KTERKDCVIV
EGVGNLMHHI ARCCQPIPGD SIVGYITMGR GISIHRCDCE QFLELQSVHP ERVVESRWGD
NYSNGFHLNI RIVASDRNGL LRDITTVLAN DKISVLGVSS RTDTKRQVAN IDMQIELNNV
EMLSKILSRL EKLDDVIEAK RL
//