ID A0A347UKI1_9RHOB Unreviewed; 709 AA.
AC A0A347UKI1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN ORFNames=BAR1_16310 {ECO:0000313|EMBL:AXX99359.1};
OS Profundibacter amoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Profundibacter.
OX NCBI_TaxID=2171755 {ECO:0000313|EMBL:AXX99359.1, ECO:0000313|Proteomes:UP000261704};
RN [1] {ECO:0000313|EMBL:AXX99359.1, ECO:0000313|Proteomes:UP000261704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAR1 {ECO:0000313|EMBL:AXX99359.1,
RC ECO:0000313|Proteomes:UP000261704};
RA Le Moine Bauer S., Sjoeberg A.G., L'Haridon S., Stokke R., Roalkvam I.,
RA Steen I.H., Dahle H.;
RT "Profundibacter amoris BAR1 gen. nov., sp. nov., a new member of the
RT Roseobacter clade isolated at Lokis Castle Vent Field on the Arctic Mid-
RT Oceanic Ridge.";
RL Submitted (SEP-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}.
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DR EMBL; CP032125; AXX99359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347UKI1; -.
DR KEGG; pamo:BAR1_16310; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000261704; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 2.
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:AXX99359.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261704}.
FT DOMAIN 48..147
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 630..704
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 709 AA; 80106 MW; 884B833D21BD28C4 CRC64;
MPDKITVDDL IALVRSYNPK TNETLIREAF AYGQAMHEGQ FRHSGEPYFT HPVAVAAILT
QQRLDDATII TALLHDTIED TKSTYTEVEE KFGKEIAELV DGVTKLTNLQ LSSTQTKQAE
NFRKLFMAMS KDLRVILVKL ADRLHNMRTI KSMRPDKQVQ KARETMDIFA PLAGRMGMQW
MREELEDLAF SVLNPEARNS IMRRFITLQK ESGDVIKKIT DDIRIELDKV GIKAEVLGRA
KKPYSIWRKM EEKGQGFSRL SDIYGFRVIT NTECDCYRVL GAIHQRWRAV PGRFKDYISQ
PKSNGYRSIH TTVSGRDGKR VEVQIRTQQM HDVAESGVAA HWSYRDGVRS ENPFAVDPAK
WVAGLTERLD ASEDHDEFLE HVKLEMYSDQ VFCFTPKGEV VKLPRGATPL DFAYAIHTRI
GDSCVGARVD GIRVPLWTRL KNGQSVEIMT AEGQRPQATW IDIAVTGRAK SAIRRSLRSE
DRERFIKLGR ELARVAFEHV GKKATDKALA TAAKRMGLVD TDELLALLGS AEMNAREVVE
GLYPELATHT GDEVELTRAV VGLEQDQTFE RASCCQPVPG ERIVGISYRG KGVVVHAIDC
PVLSEFEDQN DRWVDLHWHS GKHPAGHTVS FMMTISNDAG VLGRICTLIG EQKANIADLV
FMDRKPDFYR ILIDVDLRDV EHLHTVMTAL EADSDVAALE RYRDPARKP
//
