ID A0A370NFM7_9BURK Unreviewed; 785 AA.
AC A0A370NFM7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:RDK04407.1};
GN ORFNames=DLM46_00520 {ECO:0000313|EMBL:RDK04407.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDK04407.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) 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:RDK04407.1}.
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DR EMBL; QHKS01000001; RDK04407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370NFM7; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000254875; Unassembled WGS sequence.
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:RDK04407.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000254875}.
FT DOMAIN 95..194
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 436..497
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 689..764
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 87487 MW; E2E6238D615FF742 CRC64;
MSTTPPTATE AERDADSPSS ARKYIDAVLE QSFRHLFGPT ATPEQPRRHD VVSIAKLTSA
LSGYLQPEEI KEIKAAFHFG DEAHLGQYRQ SGEPYITHPV AVAEICAGWN LDAQAIMAAL
LHDVMEDQGV TKAELAERFG AKVAELVDGL SKLDKMEFRN REEAQAENFR KMLLAMARDV
RVILVKLADR LHNMRTLGAV PHEKRRRVAR ETLDIYAPIA HRLGLNNTYR ELQDLSFANF
NPHRYATLEK AVKAARGNRR EVVGKILESV QRAIADAKLD AEVTGREKTI FSIYKKMRDK
QLSFSQVLDV YGFRVVVESA LECYTCIGAL HALYKPVPGK FKDYIAIPKV NGYQSLHTTL
VGPFGAPIEF QVRTRKMHEI AEAGVAAHWL YKNGGADLND VQKRAHQWLK SLLDIQSEAG
DSSEFLEHVK IDLFPDAVYV FTPKSKIMAL PRGATALDFA YSIHSDLGNQ CVAVKINNEL
LPLRTELKSG DIVEVITAPY SKPNPAWLGF VRTGKARSAI RHYLKTMRLN ESVQLGERLV
DQALKGYGLA LSDVTPEAWE KLVQWTGNKN RQEIFADIGL GRRVAAVMAK RIEVLMSGRD
ADDDGSRSDG SAPHAPPVVI TGTEGMSVQL SACCRPIPGD DIMGYIGIGL GMAIHTTDCR
VAQRIHRRDP GRWIDVAWAP QPGRLFDVAV KVLVKNTKGV FARVAADITS ADANIVHIAM
DEDLSQESTV LRFVIQVSDR VHLANVMRRV RTNPDVMRIA RERPSEEGHH RHEGGMRIDR
ERADY
//
