ID A0A143HQ69_9GAMM Unreviewed; 705 AA.
AC A0A143HQ69;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN ORFNames=A3224_15905 {ECO:0000313|EMBL:AMX03874.1}, SAMN05660479_01230
GN {ECO:0000313|EMBL:SFC14221.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03874.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|EMBL:AMX03874.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX03874.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFC14221.1, ECO:0000313|Proteomes:UP000181967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFC14221.1,
RC ECO:0000313|Proteomes:UP000181967};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00024273};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC 1/1. {ECO:0000256|ARBA:ARBA00024329}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP014864; AMX03874.1; -; Genomic_DNA.
DR EMBL; FOKT01000003; SFC14221.1; -; Genomic_DNA.
DR RefSeq; WP_067156912.1; NZ_JAPHQH010000003.1.
DR AlphaFoldDB; A0A143HQ69; -.
DR STRING; 252514.A3224_15905; -.
DR GeneID; 76609513; -.
DR KEGG; mthd:A3224_15905; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000076077; Chromosome.
DR Proteomes; UP000181967; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SFC14221.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW Transferase {ECO:0000313|EMBL:SFC14221.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 390..451
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 633..705
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 195..222
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 705 AA; 79113 MW; 1B483199EF69187C CRC64;
MHTIDSLAHR LSSYLPPNQI QIVRRAYFYA EQAHDGQQRR SGEPYITHPL AVATILAGMH
MDHQSLAAAM LHDVIEDTGI PKAALAEQFG DEVADLVDGV SKLTQFETDS PAEKQAENFQ
KMALAMARDI RVILVKLADR LHNMRTLGAL KPQKRARIAR ETLEIYAPIA NRLGMNDVRI
EFEDRAFFAI HPLRASRLRA ALVAARGNRK ELLEQIQNAI ELRLQREGID ALVIGREKHL
YSIYQKMRAK KKSFKEIMDV YAFRIIVDSV DTCYRVLGVM HNLYKPVISE FKDYIAIPKS
NGYQSLHTVL LGMHGVPIEV QIRTKEMDEM ANSGIAAHWL YKASGDEVIN TGGTSQVRAR
RWVQGLLEMQ QRAGNSLEFI ENVKIDLFPD EVYVFTPKGE IIDLPAGATA VDFAYSVHTD
IGNSCVAVRI NQRLAPLSQP LESGQKVEIL TRKNAQPNPN WLNFVVTAKA RSAIRHFLKH
QRHHDSVALG RRLLEKALGK FNTRLEDLTE EQLQKGLQEN KVPTLEKLLE EIGLGNKVAF
SAAKLLAPEG SEETEASHIS SPLTIDAEEG MLISFARCCR PIPGDTIVGH ISSGKGVVVH
RDTCRNTIDF REHPENIMLV NWSPDVKGEF LGDVRVEVES ERGIIAQLAT RITEEGASIE
QIHVDEKDAH NSVISLTLEV SNRVHLARVM KRLRNLPAVI RISRP
//
