ID D1AH20_SEBTE Unreviewed; 721 AA.
AC D1AH20;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACZ08054.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ACZ08054.1};
GN OrderedLocusNames=Sterm_1186 {ECO:0000313|EMBL:ACZ08054.1};
OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Sebaldella.
OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ08054.1, ECO:0000313|Proteomes:UP000000845};
RN [1] {ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Eisen J.A.;
RT "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ08054.1, ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX PubMed=21304705;
RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Chen F.;
RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT 11300).";
RL Stand. Genomic Sci. 2:220-227(2010).
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; CP001739; ACZ08054.1; -; Genomic_DNA.
DR RefSeq; WP_012860650.1; NC_013517.1.
DR AlphaFoldDB; D1AH20; -.
DR STRING; 526218.Sterm_1186; -.
DR KEGG; str:Sterm_1186; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_0; -.
DR Proteomes; UP000000845; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000000845};
KW Transferase {ECO:0000313|EMBL:ACZ08054.1}.
FT DOMAIN 49..147
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 384..445
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 647..721
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 721 AA; 83696 MW; C96F5AC8C3C07369 CRC64;
MRIIKERFAE LEKKIKENNL DVDVDKIENA FVLAYESHVG QKRKSGEDYI LHPIEVAEIL
VDLRLDTDTI VAGILHDVVE DTLITIPDIE YNFGKEVARL VDGVTKLRNL PRTDSSKRIE
NIRKMVVAMS EDIRVVLIKL ADRLHNMRTL KYMKPEKQIE KAKESLEIYA PIAHRIGMAK
IKWELEDISF RYLYPEKYKE ISTLVKTKRK EREKYTNEVI EKISGELKKF NIQGEVTGRP
KHLYSIYKKM VEKQKNFNDL HDLIAIRILV NKEVECYNVL GIIHSLYIPV AGRFKDYIAV
PKSNGYQSIH TTIEGPDKQN IEVQIRTYAM HMIAEEGVAA HWKYKEKKSK SKDENYYAAV
KKMIAGNENV DSFVKEVTDN VLNETIFVFT PKGDVIELQN AATPLDFAFH IHTQIGYKTV
GAKVNDKIVP LDYELKNGDK IEILTSKNSK GPGKDWINMV KANSSKVKIR KWFKDKEFEE
RTKDGELLLE RELEKINLKF KDIEEDEKLF LYMKKYNIND TKSLFYKFAT GELSLEGFTN
RFEVKKELDE KQVLEEETLK GNKRKEKSTG GIRISGTDNT MYKFAKCCTP LPGDDIQGFV
TKVRGIVIHR KDCKNLHNLL KNDPDRAIDV EWDVEEIGKS TSKYEFVFTA KALNRPNILM
DIIKVLNDFK MDLINVNTTV TKENGIEYSL MKFDIMIKKR DDFDRLANNL KSMKDIVDII
R
//