ID B9M903_GEODF Unreviewed; 716 AA.
AC B9M903;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=GTP/GDP 3'-pyrophosphokinase and (P)ppGpp 3'-pyrophosphohydrolase {ECO:0000313|EMBL:ACM20499.1};
GN Name=relA {ECO:0000313|EMBL:ACM20499.1};
GN OrderedLocusNames=Geob_2145 {ECO:0000313|EMBL:ACM20499.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM20499.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM20499.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM20499.1; -; Genomic_DNA.
DR RefSeq; WP_012647228.1; NC_011979.1.
DR AlphaFoldDB; B9M903; -.
DR STRING; 316067.Geob_2145; -.
DR KEGG; geo:Geob_2145; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_7; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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 Hydrolase {ECO:0000313|EMBL:ACM20499.1};
KW Kinase {ECO:0000313|EMBL:ACM20499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW Transferase {ECO:0000313|EMBL:ACM20499.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 642..716
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 716 AA; 81502 MW; 61C5116FD4B1E6E3 CRC64;
MIRLNDILEK VSSYNPSCDL ELVRKAYVFC AKVHQGQTRL SGEPYLVHPM EVAGVLAELK
LDVPTVVTGL LHDTVEDTLT TLEELEEMFG PEVARLVDGV TKIGKIHFKT KEESQAENFR
KMLLAMANDI RVILVKLADR LHNMRTLQYQ PEPKQRSIAK ETLDIYAPIA NRLGISWVKS
ELEDLSFRYL DPQIYYDLAS KVTKKKKERE TYVDEVMQII KAKLVDHGIK GEVSGRSKHL
YSIYRKMQSR SVDIDEIYDL IAIRVMVEDI RECYEVLGII HSTWKPIPGR FKDYIAMPKG
NMYQSLHTTV IGPYGERMEV QIRTSEMHRV AEAGIAAHWK YKEGKGYDEK EVKRFTWLRQ
LLEWQQELDD SREFMDTVKV ELFPEEVYVF TPKGDVKGYP KGSTPIDFAY SVHTDVGHRC
VGAKVNGKLV PLKYELKNGD IVEVITSPHH TPSKDWLKIV RSSRARNKIR AWIKTEERLR
SITLGREICE KEFRRYSQNF SKVQKTGELK RVVGEFGFVG EDDLMAAVGY GKLSCQQILG
KLFPAEKFEE AQDRKETRVG KVIQKLKGKS SSAIQISGVD DVLVRFGKCC NPLPGDDIVG
FITRGRGVTV HTADCPFALD SDPQRRIDVA WNKGKKTALP VKMRIACHDE KGILANITTA
ITNCEANIVS ASIQSTVDKR GINTFEVDVT DLDHLNRVFN SVMKVKGVIK VDRLKS
//
