ID B3QL47_CHLP8 Unreviewed; 731 AA.
AC B3QL47;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACF10835.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACF10835.1};
GN OrderedLocusNames=Cpar_0412 {ECO:0000313|EMBL:ACF10835.1};
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=517417 {ECO:0000313|EMBL:ACF10835.1, ECO:0000313|Proteomes:UP000008811};
RN [1] {ECO:0000313|EMBL:ACF10835.1, ECO:0000313|Proteomes:UP000008811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327 {ECO:0000313|Proteomes:UP000008811};
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., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001099; ACF10835.1; -; Genomic_DNA.
DR RefSeq; WP_012501668.1; NC_011027.1.
DR AlphaFoldDB; B3QL47; -.
DR STRING; 517417.Cpar_0412; -.
DR KEGG; cpc:Cpar_0412; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_10; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000008811; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; 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; 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; PS50889; S4; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000313|EMBL:ACF10835.1}.
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 658..731
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 731 AA; 83355 MW; 184F05EE6F2AB0A2 CRC64;
MLAQIEQEHY QKLHEILRLC RANLKNYDES LIQRAFFMCY RAHEGEKRAS GEPFFYHPVE
VAKLLVTELP LDGVSVAAAL LHDVIEDSGY TYEDIAAELG TEVADIVEGL TKISGIMVNR
ETTEAEGFRK MLLSMVKDIR VILIKFCDRL HNMRTLDSLP EHRRLRMALE TRDIYAPLAH
RFGLGKMKVD LENLAFKYID PKMYDYLLKK VRLSRNERMA YLNKMIAPIK DDLEKQGFNV
EVQGRAKHLF SIYNKMRLKN KQFDDIHDLY GIRVIIDTDK LSDCFAVYGY ITQKYPPIPQ
HFKDYISIPK HNGYQSLHSA IIGPKGHVIE LQIRTRRMHE FAELGVAAHW RYKEKISKDD
AAVDSFLKWA RELIKDADTA SAFMEGFKLN LYHDEIYVFT PKGDMKILPA GATPIDFAYA
IHTEIGNGCI GAKVNGKIVR LNAELRSGDR VEVITSKNQK PKPDWLKIVV THRAKLKIRA
AINEERRKEI EKGRNIFDKM LTGTKRLFTE NDAIRAIRKH GIKTPADLFS ALANQQISSE
EVMESITRPH GKGAEHEGDV QGKAPHKEFA EIAREVQERP TSHKDEVTIA GMNNIAYSYA
KCCNPVPGDD IIGFVTTEGA VKIHRKNCFN VTNENSVKSE RIVSVAWNRK LNTEFLAGIR
IVGEDKVGMT NQITGVISKF DTNIRTITLH AKDGIFVCNL MIFVKNTDKL TTLMDKLKKV
QGVFTVERMS A
//
