ID F2NBI8_CORGP Unreviewed; 784 AA.
AC F2NBI8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:AEB06724.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:AEB06724.1};
GN OrderedLocusNames=Corgl_0610 {ECO:0000313|EMBL:AEB06724.1};
OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Coriobacterium.
OX NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB06724.1, ECO:0000313|Proteomes:UP000006851};
RN [1] {ECO:0000313|Proteomes:UP000006851}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC {ECO:0000313|Proteomes:UP000006851};
RX PubMed=23961308; DOI=10.4056/sigs.3507020;
RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL Stand. Genomic Sci. 8:15-25(2013).
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}.
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DR EMBL; CP002628; AEB06724.1; -; Genomic_DNA.
DR RefSeq; WP_013708467.1; NC_015389.1.
DR AlphaFoldDB; F2NBI8; -.
DR STRING; 700015.Corgl_0610; -.
DR KEGG; cgo:Corgl_0610; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000006851; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000006851};
KW Transferase {ECO:0000313|EMBL:AEB06724.1}.
FT DOMAIN 78..177
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 428..489
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 699..773
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 589..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 87474 MW; BFD26FF8849C0C34 CRC64;
MDAKTRAEHD ASLQPFSEMM NYTRADDLPP EIIADNCEKL IQLCRRYMSV EDSDLVERAY
CFAAERHENQ KRRSGELYIN HPVEVAIILA ELKMDCDVLC AALLHDTVED TQTSLDEVAS
LFGSTVSELV DGVTKLTNIE VGSMDEKQAL NLRKMFLAMS RDIRVIIVKL ADRLHNMRTL
AALSEDRRLF KARETMDVYA PLADRLGMSS IKWELEDLSF FYLDPEAYQR ISRMVAESRE
VRERFLSETI KTLTDELKKM GMGDYQISGR SKHYWSIHQK MRRKGKEFSE IYDLVALRVI
APSMNDCYLT LGAIHSLWHP MPGRFKDYVA TPKLNNYRSL HTTVIGPTAR PLEIQIRTAE
MHEQAEYGIA AHWLYKKSGG CASLKSKEAQ RQDEQINTLR HSLDWAASDD IEDAKEFLRT
LKADLFDQEI FVFTPKAEVM SLRAGATPLD FAYAVHTEVG NHCVGAKING AVAPLTHRLS
MGERVEILTN KSAKPSRDWL AIVNTPSAKS KIRRYFAMAT KDDDAASGRD ILARDLRRRG
YGISTARSTR ALTQIAEQLK YKQLADLFAA IGAGKLAARS VGNKVERLLD PKPLGEKTAS
GGALSTPAPS RGSRRSPQQE QHRSCGVRMK GSDSGDILIH LAHCCNPVAG DDIVGFITHG
RGVSVHRASC PNVKGLMEHA ERMTAVEWDC AADALFRVEV VVECLDRMGL LKDVTIAIGD
AGGNILSAST STTREGIAVL RYLVEISDAS GLDPLFAAIT RVESVYDARR IMPGEGGEQM
KRRS
//
