ID S8GRP2_9BACT Unreviewed; 760 AA.
AC S8GRP2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EPT34400.1};
GN ORFNames=HMPREF9012_0769 {ECO:0000313|EMBL:EPT34400.1};
OS Bacteroidetes bacterium oral taxon 272 str. F0290.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=888054 {ECO:0000313|EMBL:EPT34400.1, ECO:0000313|Proteomes:UP000015345};
RN [1] {ECO:0000313|EMBL:EPT34400.1, ECO:0000313|Proteomes:UP000015345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0290 {ECO:0000313|EMBL:EPT34400.1,
RC ECO:0000313|Proteomes:UP000015345};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPT34400.1}.
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DR EMBL; AUTU01000009; EPT34400.1; -; Genomic_DNA.
DR AlphaFoldDB; S8GRP2; -.
DR PATRIC; fig|888054.3.peg.407; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000015345; Unassembled WGS sequence.
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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015345}.
FT DOMAIN 408..469
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 760 AA; 87073 MW; 56D8BFC090BB6888 CRC64;
MPSEAKIQEQ LEDKMINDAF QELLNAYLAT KHRKRTEIIT KAFSFAKQAH KGVRRRSGEP
YIMHPIAVAK IVCTEIGLGS TSICSALLHD VVEDTDYTVE DIENLFGPKI AQIVDGLTKI
SGGIFGDRVS AQTENFKKLL LTMSDDIRVI LIKMADRLHN MRTLGSMLPS KQYKIAGETL
YIYAPLANRL GLNKIKTELE DLSFRYEHPE TYKEIQHKLK ETQAEREKLF DNFTAPIREQ
LDKIGIKYRI VARIKTPYSI WNKMQTKHVS FEEIYDILAV RIIFTPKDIE EEINECFNIY
VNITKIYKPH PDRLRDWVSH PKSNGYQALH VTLMSNKGQW IEVQIRSERM NDVAEQGFAA
HWKYKEGGYT EDQGELDKWL HTIKEILDDP QPDAMDFLDT IKLNLFASEI FVFTPKGELK
TMPQNCTALD FAFSIHTFLG SHCIGAKVNH KLVPMSYKLK SGDQVEILTS NSQHVQPSWI
NFATTAKAKS KILAILRREQ RSAQQDGEEM LQEFFDETEI ENTSTNIKKL CDFHRLDTPE
ELFAAIGRKD IVLGENDKNE LKEKSSGKNW KKYITFAFGN KSNKNGKKVE EEKAEATVSK
IDNKQIITLT EDDDIQKNYI IANCCKPIPG DDVLGFIDDK NHIVIHKRQC PVATKLKSGY
GNRLLAVNWE PGKSVYFSVF LYIKGIDRIG VLNRVTQLIS DRLNVNIHRL TIHTNDGIFE
GRIELFVHDV NDVKIILSTL KKIAEIKTVT RIDQFDAVPT
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