ID A4BBK5_9GAMM Unreviewed; 744 AA.
AC A4BBK5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=MED297_00925 {ECO:0000313|EMBL:EAR10340.1};
OS Reinekea blandensis MED297.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR10340.1, ECO:0000313|Proteomes:UP000005953};
RN [1] {ECO:0000313|EMBL:EAR10340.1, ECO:0000313|Proteomes:UP000005953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED297 {ECO:0000313|EMBL:EAR10340.1,
RC ECO:0000313|Proteomes:UP000005953};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (FEB-2006) 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:EAR10340.1}.
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DR EMBL; AAOE01000004; EAR10340.1; -; Genomic_DNA.
DR RefSeq; WP_008046535.1; NZ_CH724153.1.
DR AlphaFoldDB; A4BBK5; -.
DR STRING; 314283.MED297_00925; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000005953; Unassembled WGS sequence.
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; 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 Kinase {ECO:0000313|EMBL:EAR10340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005953};
KW Transferase {ECO:0000313|EMBL:EAR10340.1}.
FT DOMAIN 415..476
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..742
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 744 AA; 84049 MW; 2252170D25A72DF0 CRC64;
MKVREDQPVF SDGTVDLEAW LERIEAKTAI VDPEELIRAC RIARTAEQES DHPANTWGEG
ASAFKTGLEM VEILADLGLD QDALVAAVLY RTVREEELAL ETVRDQFGPK IANLIQGVMR
MAAISNRKST RDSVFGQNET QGEAVRKMLV AMIDDVRVAL IKLAERTCAI RAIKHSPAAR
RYRVAREVFD IYAPLAHRLG VGHLKWELED LAFRYIEPQD YKKIAKLLDE KRLDRQEYIQ
KVQTLITEEI EKANVQAEIQ GRAKHIYSIW RKMKRKNITF SQVYDIRAFR ILVPEVRDCY
TVLGIVHSMW RHIPREFDDY IASPKQNGYR SLHTAVIGPE GKVVEIQIRT QEMHDDAELG
VCAHWLYKGT DAKKGGQSRG YEEKVSWLRQ VLEWHDELGG IDEMVEELGV DVTIDRIYVL
TPDGHVVDLA SNATPIDFAY KVHTDIGHRC RGAKVNGRIV SLNTQLKIGD QVEILTGSEA
SPSRDWLNSD LGYVTSSRAR AKIKHWFKSQ DRDINVRDGR DMLLRELRRF NLTDVDMQAL
AQDVNFTDED SLFAALGAGD IRLMHVVHHA EELTHPKKAK APAFKTPKKQ NHSGDLIIQG
VGNMLTTIAN CCKPVPGDPV VGFITQGRGV SIHRDDCVNL LQLKSTEPER IIDVSWGNEV
KTTYPVELLV SAYDRTGLLK DLMVVLANIG INVISMNTLS NKNDNSAKMT ITVEVEDLRS
LGRIMTQLSK VPNVADVHRI YTKS
//
