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Database: UniProt
Entry: E6KZU7_9PAST
LinkDB: E6KZU7_9PAST
Original site: E6KZU7_9PAST 
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
//
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