ID A0A0K1K4F4_9BURK Unreviewed; 758 AA.
AC A0A0K1K4F4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:AKU24282.1};
GN ORFNames=ACZ75_25310 {ECO:0000313|EMBL:AKU24282.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU24282.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU24282.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU24282.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-2015) 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; CP012201; AKU24282.1; -; Genomic_DNA.
DR RefSeq; WP_050411966.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1K4F4; -.
DR STRING; 1678028.ACZ75_25310; -.
DR KEGG; mnr:ACZ75_25310; -.
DR PATRIC; fig|1678028.3.peg.5136; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000056897; 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:AKU24282.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056897}.
FT DOMAIN 92..191
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 433..494
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 683..755
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84246 MW; 2C3127197E3557E0 CRC64;
MNLSETSISD QPASRAKRPA KSAPGVDPSA ASSIPTSPLA APVVAAGVAT ISHLSEKLAE
YMTPADLKKV REAYRFSDEM HLGQVRKSGE PYISHPIAVA EICADWKLDA QAIMAALLHD
VMEDQDVKKD ELIERFGAPV AHLVDGLSKL EKIEFQSQIE AQAENFRKML LAMASDVRVI
LIKLADRLHN MRTLEVMAPA KKRRIAGETM EVYVPIAHRL GLNNIYRELQ DLAFSHLYPL
RYHVLSKAVK AARGNRREVV KKILESVKNT LGMAGISAEV YGREKTLYGI YKKMRAKHLS
FSQVLDVYGF RVVVDSFANC YVALGTLHSL YKPMPGKFKD YIAIRKLNGY QSLHTTLIGP
YGTPVEFQIR TQEMHRTAES GVAAHWLYKN SDANMSDLQQ RTHAWLQSLL DIQQQTGDSA
EFLEHVKVDL FPDSVYVFTP KSKIIALPRG ATPIDFAYAI HTGIGDHTVG VNINGEAAPL
RTELRNGDII EIVTDNSSRP SPTWLSFVRT GKARSAIRHH LRTINLPESI RLGQQLLNQA
LHAINIDPQL PDNLTERLLN ESSAKSLDEL YADIGIGKRM AALVARHIFG MLGGEAASAP
VDHTSAAELD PVTIYGSEGV SVQLAPCCLP IPGDQIVGQL RRDQGLQVHT GDCTVAKRQR
QKEPDRWIAV KWAPELNRRF DTRIKLLINN EKGILARVAA EIGESDGNIT FVGMDEDKEH
ILHQLRFTIQ VKDRVHLAGL LRNVRRVAGV NRVSRERA
//
