ID A0A011NYG5_9PROT Unreviewed; 752 AA.
AC A0A011NYG5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EXI69675.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:EXI69675.1};
GN Name=relA {ECO:0000313|EMBL:EXI69675.1};
GN ORFNames=AW08_00168 {ECO:0000313|EMBL:EXI69675.1};
OS Candidatus Accumulibacter adjunctus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI69675.1, ECO:0000313|Proteomes:UP000020218};
RN [1] {ECO:0000313|EMBL:EXI69675.1, ECO:0000313|Proteomes:UP000020218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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 -!- 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:EXI69675.1}.
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DR EMBL; JFAX01000001; EXI69675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011NYG5; -.
DR STRING; 1454001.AW08_00168; -.
DR PATRIC; fig|1454001.3.peg.350; -.
DR Proteomes; UP000020218; 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; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
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; 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:EXI69675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW Transferase {ECO:0000313|EMBL:EXI69675.1}.
FT DOMAIN 424..486
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 681..752
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 752 AA; 83814 MW; C7628FD81F60C235 CRC64;
MNGQRRPYNR PMVSVLHSLA AHGDPAQSLQ ALGEGLPAAA TDRLWRAVEY ARAVYGDRLL
GSGEEVWGHA LGMALIVAGL KLDADSRLAA LLFAVPALQE RGLAQIESSF GSGVAHLVGG
ISRLDRMRPI TRKFSAHSAA SAESNPQEMK AQVEILRKML LATVEDIRVV LLRLASRTQT
LRHFAAEADE LRVPVARETL ELYAPLANRL GVWELKWELE DLSFRFLHPE IYKDIARHLD
EKRVEREQFI ATASARLQEE LQAAGVAHAE VYGRPKHIYS IWNKMRKKGV GFAEVYDVRA
LRVIVDEVRD CYTALGIVHH IWSPIAREFD DYIAHPKGND YRSLHTAVHC ADGRALEVQI
RTRDMHRHAE LGVAAHWRYK EGGRATPEDR YDEKIAWLRQ LLTWREEVAD ASDWVRHYKE
AAFDETVYVL TPQGRVVDLP RGATPVDFAY RVHTDVGHRC RGAKVDGALV PLNTQLATGQ
RVEIVLAKQG GPSRDWLNPT LGYLFTHRSR LKVRQWFASL ALDDTLAEGR ALVQRELQRL
GQPGLNLDDL AVRLGLARSD DLFIAMARAT LNMRQLQAAV RASEEPVEDR VPDELTVRRQ
RDSDVAEKGI LIVGVGRLLT QLAGCCKPAP PDPIVGFVTR GRGVSVHRAD CSNLVNLQAM
HPERLIETSW GAGSEAVFAV DIVIDAHDRQ GLLRDVSDVL ARERINVIAV NTQSRQGNAH
MSFTAEVSSI PQLERTLALL HAVHGVVGAR RA
//
