ID A0A0D8HGA8_9ACTN Unreviewed; 740 AA.
AC A0A0D8HGA8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Bifunctional (P)ppGpp synthase/hydrolase RelA {ECO:0000313|EMBL:KJF16879.1};
GN Name=relA {ECO:0000313|EMBL:KJF16879.1};
GN ORFNames=AXFE_23000 {ECO:0000313|EMBL:KJF16879.1};
OS Acidithrix ferrooxidans.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidithrix.
OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF16879.1, ECO:0000313|Proteomes:UP000032360};
RN [1] {ECO:0000313|EMBL:KJF16879.1, ECO:0000313|Proteomes:UP000032360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF16879.1,
RC ECO:0000313|Proteomes:UP000032360};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT strain Py-F3.";
RL Submitted (JAN-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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
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:KJF16879.1}.
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DR EMBL; JXYS01000072; KJF16879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8HGA8; -.
DR STRING; 1280514.AXFE_23000; -.
DR PATRIC; fig|1280514.3.peg.3021; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000032360; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:KJF16879.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000032360};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 55..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 390..451
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 653..727
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 82770 MW; 0E5CCA83EE3EFEDD CRC64;
MVPGISAEFE TVLLDKLLRS FRARRPEAPS GFIESAFASA IRAHEGQFRR SGEPYVTHPI
AVSQIVTDLG VDEVTIVAAL LHDTVEDTSI ELDQISTRFS PEVAAIVDGV TKLDRLSFDS
KEAQQAATVR KMIIAMAKDP RVLIIKLADR LHNMRTLAVL PEWKQRRIAQ ETIDIYAPLA
HRLGIQEIRW QLEDLAFAVL QPRRYAEIEQ MVQLRTPERE QSIGLLLKNL KDRLLDAGVV
ADVKGRPKHF WSIYEKMVVK TKEFNEIYDI IGIRIICETE KDCWASLGVV HSLWNPIPGR
FKDYINTPKF NLYQSLHTTV VAPGGNPLEV QVRTFEMHQR AEFGIAAHWG YKEGSSNSEM
AWLGRILDWQ KDTPDPIEFL ENLKLDLELD EVYVFTPKGK VVSLPAKATP IDFAYTIHTE
VGHRCIGAKV NGRLVPLDSV LKSGDTVEIF TSKVESAGPS RDWQSIVVTP RARSKIRHWF
SRERREDALE SGRDELIKAL RKEGLPVQKM AASDTLGKLA VSLGFSDVEA LYVSVGEGHA
SAKGLAQRVV REMAPEESEI QLPTTVNPSR RQSKRRRTPG VYVEGLDDVV IRFSRCCSPV
PGDDIIGFVT RGRGVSVHRT NCSNAAALAA SSRERLIEVE WDSDISNSVF SAQIEIRALD
RSRLLADVAR VLSEHHLNIL SSSTQAGVDR ISRMRFEFEL ADPSHLDSVL SALRKLDSVY
DAYRVVEGGH GEGDLGGNLN
//
