ID A0A410GB25_9BURK Unreviewed; 758 AA.
AC A0A410GB25;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:QAA93493.1};
GN ORFNames=CKA81_06305 {ECO:0000313|EMBL:QAA93493.1};
OS Pollutimonas thiosulfatoxidans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=2028345 {ECO:0000313|EMBL:QAA93493.1, ECO:0000313|Proteomes:UP000283474};
RN [1] {ECO:0000313|EMBL:QAA93493.1, ECO:0000313|Proteomes:UP000283474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ye3 {ECO:0000313|Proteomes:UP000283474};
RA Park S.-J., Kim H.;
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022987; QAA93493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410GB25; -.
DR KEGG; pus:CKA81_06305; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000283474; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
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; 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; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 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 Hydrolase {ECO:0000313|EMBL:QAA93493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283474}.
FT DOMAIN 91..190
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 432..493
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 684..758
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84133 MW; C5807B95CB863DC6 CRC64;
MAFSGLRGAS SGLLAVLKKG PRLRRNKNAK PAAPRPGTPE NSGPNTIASL APLTKIISHY
LSPKDVERVK EAYRFSDQAH LGQFRASGEP YISHPITVTE ICAGWKLDAD SLMAALLHDV
IEDQGVTKQE LAEKFGPDVA EIVDGLSKLD RLEFATKAEQ QAESFRKMLL AMARDVRVIL
IKLADRLHNM RTLDAVTPEK RRRIARETLE IYTPIAHRLG LNALFRELQD LCFQAIHPNR
YQVLHKAMMA ARGNRREVLS KITDAVQVAL PAAGIEAEVS GREKSLYSIY TKMAEQKKSF
SDVLDIYGFR VIVHTLPECY LALGTLHQLY RPVPGKFKDY IAIPKLNGYQ SLHTTLVGPY
GTPVEFQFRT RDMDHIAEEG VASHWLYKED NVTLNDLQKR THQWLQSLLD IQSQTGDSGE
FLEHVKVDLF PDAVYVFTPQ GKIISLPRGA TPVDFAYTIH TDIGNQAVAS KINGEFAPLR
TELKSGDSIE IITSPASRPS AQWLNYVRTG RARSEIRHYL RTVKYEESVA FGQRLLNQAF
DQLHLPHPAE DDPEWEKLAK SSGAASREEI LADIGLGKRL AAVVARRFAP ENALLATTAA
AVDEFTSSVN APILIHGNEG QAVQLAPCCG PLPGDAIIGG IRLGHGLVVH MDECAVAQRQ
RAREPERWIP VMWDTNTARH LSTRLDVTVV NERGVLGRLA AEVTEADSNI MHLTMQDDAA
ATGVLHITVQ VDSRKHLAQV IRAMRHVPQV QKIVRVKG
//
