ID B3QV22_CHLT3 Unreviewed; 744 AA.
AC B3QV22;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACF12976.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACF12976.1};
GN OrderedLocusNames=Ctha_0505 {ECO:0000313|EMBL:ACF12976.1};
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC Chloroherpeton.
OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF12976.1, ECO:0000313|Proteomes:UP000001208};
RN [1] {ECO:0000313|EMBL:ACF12976.1, ECO:0000313|Proteomes:UP000001208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
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., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
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}.
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DR EMBL; CP001100; ACF12976.1; -; Genomic_DNA.
DR RefSeq; WP_012499060.1; NC_011026.1.
DR AlphaFoldDB; B3QV22; -.
DR STRING; 517418.Ctha_0505; -.
DR KEGG; cts:Ctha_0505; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_10; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000001208; 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 Reference proteome {ECO:0000313|Proteomes:UP000001208};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000313|EMBL:ACF12976.1}.
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 670..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 744 AA; 85050 MW; 0E75E41639E5AF85 CRC64;
MLAQIEEDHY VKLNEILSLC KEKLYHYDEA LIRKAFFLCY RAHSEEKRAS GEPFFFHPVE
VAKILLTEIP LDSVSVAAAL LHDVVEDTDY TYEDLQDEFG DEIASIVAGL TKISGIFDNR
EIKEAESFRK MLLSVIHDIR VILIKFCDRL HNMRTLDALP PHRQIRIAIE TRDIYAPLAH
RFGVGRIKIE LENLALKYID REAYDEIVQK LQMTRPERER YLESVMSPIR KKLNELNFEY
NMSGRPKHVF SIYNKIQQRG KSFEDIYDIY GIRIILHSET NADCYNVYSR ITELFSPVPD
RFKDFISVPK HNGYASLHTT IVGPGGRMIE VQIRTEKMNE IAETGIAAHW RYKEKTKERD
KAIDELIKWA REFIENSSMS STVMDSDSAT SFMEGFRMHL YQDEIYVFTP KGDMKTMPVN
ATPVDFAFEI HTEVGMRCIG AKVNGKIVSL NSKLKSGDQV EIITSKNQTP KADWEKFVVT
HKAKIKIKQA LNEERRTEIE KGRGIWNRVL TKTKSIIALT ERDLLKAIKE HGFHFNTPAD
FYRGLATDKI NAEEVLNNLN EKKKSPPQKE LTPLTGEAQA NTLKKLREPS INQKNKDAVR
IEGLPGIAFE YARCCNPVPG DDIIGLLSVG SKAVKIHRRN CRSLTSDKLA TMKLLDACWE
KDNNGQFLAG LKILGEDVIG MTNKITEVIL KSDINIRSIS LDASDSLFEG NVLLYVKDVA
TLNRLAEKIK RIKGILSVGR LSNE
//
