ID A0A2N1F800_9FLAO Unreviewed; 738 AA.
AC A0A2N1F800;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:PKH51062.1};
GN ORFNames=CXF68_10365 {ECO:0000313|EMBL:PKH51062.1};
OS Tenacibaculum sp. Bg11-29.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH51062.1, ECO:0000313|Proteomes:UP000233844};
RN [1] {ECO:0000313|EMBL:PKH51062.1, ECO:0000313|Proteomes:UP000233844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH51062.1,
RC ECO:0000313|Proteomes:UP000233844};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) 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:PKH51062.1}.
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DR EMBL; PJBB01000003; PKH51062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1F800; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000233844; 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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233844}.
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 738 AA; 83846 MW; 5FB0ABC734B07226 CRC64;
MSYNATIEEE NKEIANRYKN LLKGTYQTLS EDDKKLIRKA FDIAVEAHSE QRRKTGEPYI
FHPIAVAKIV ADEIGLGATS IAAALLHDVV EDTPYTIDDM ERLFGENIAR IVSGLTKISS
LKKEQDYSIQ AENFRKMLLT LHDDVRVILI KIADRLHNMQ TMDAMPPHKQ VKIASETLYI
YAPLAHRLGL YNIKTELEDL GLKYTEPEVY KDILTKIKDS KEDQQKYINS FTGILKEALD
KEGFNYDIKG RFKSIFSIRK KMQKQNVTFD EVYDKFAIRI IYEPTSGDEK FDAWKIYSIV
TDFFKPNPAR LRDWISQPKS TGYEALHITV IGPQAKWVEV QVRSERMDEI AEKGYAAHFK
YKQNDVKENG LDGWLNRLKE TLENQSINAI DFVEDFKLNL YAKEIYVFTP KGDLKSLPKN
ATALDFAFSV HTDVGLKCRG AKVNGKLVPL SHALKSGDQV EVLTASNNKP NVRWLDFVLT
ARARTKIKSA LKAEEKIIAE EGKAILLRKL RHLKIGSGEK IIHELANYFG LKTSFDLFFR
VGNGAIDNTQ LKEFVAQRSG LIMGFIKSTF RRSPSKGFSE KEEVTHKYDA LVFGKDEQTL
DYTLAKCCSP IPGDKVFGFV TINEGIKIHK NDCPNAISLQ SNYAYRIMPA KWIDSTKQDF
TAILHLSGID NKGIVNNITR IISNSMDVFI HSINISGDHG VFDGKLSLSV KNKAQLNKLI
DNMKKLEGVQ KVERVNTL
//
