ID A0A1X9Z6B5_9SPHI Unreviewed; 735 AA.
AC A0A1X9Z6B5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:ARS40797.1};
GN ORFNames=CA265_14485 {ECO:0000313|EMBL:ARS40797.1};
OS Sphingobacteriaceae bacterium GW460-11-11-14-LB5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=1986952 {ECO:0000313|EMBL:ARS40797.1, ECO:0000313|Proteomes:UP000194429};
RN [1] {ECO:0000313|Proteomes:UP000194429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAY-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}.
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DR EMBL; CP021237; ARS40797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Z6B5; -.
DR KEGG; sbx:CA265_14485; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000194429; Chromosome.
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; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000194429}.
FT DOMAIN 61..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 735 AA; 83606 MW; 297B7C72936583DC CRC64;
MKTELVIDLE AEKQEILKRY RALLRASKST LQKGDKKEIR KAFDMALESH KDMRRKSGEP
YIYHPIAVAQ IAAEEIGLGT TSIVCALLHD VVEDTDITLE DIEREFGKKT AKIIDGLTKI
SGVFDTNSSL QAENFRKMLL TLADDVRVIL IKLADRLHNM RTMDFMPRHK QLKIASETIY
LYAPLAHRLG LYAIKSELED LSMKYLDPDT YKFIAKKLNE KKAERALFIK KFVEPIDEIV
HEQGLVADVY GRPKSIHSIW NKMKKKNIPF EEVYDLFAIR IILDSAPENE KADCWKAYSI
VTDLYRPNPD RLRDWVSSPK GNGYESLHTT VMGPRGQWVE VQIRTQRMNE IAEKGFAAHW
KYKESSNDNG LDQWIQKVRE MLSNPEANAL DFLDDFKMNL FSDEIFIFTP KGALIQLPLG
ATALDFAFEI HTDVGATCIG AKVNHKLVPI SYKLQNGDQV EIITSSKQTP KEDWLNVVVT
AKAKSKIKSS LKEEKRKIAE NGKEILERKL KSLKITYNTD NLQKLSYFFK LPSTQELFVN
VALGKIELKD IKEYLSSEKE VENRGPERPE NLSVDGIKSK IKGGESDILL IGEDMQRIDY
TLAACCNPIP GDDVFGFITV SEGIKIHRTN CPNAAQLMAN YGYRVVKAKW NKQQELTFLT
GLRIVGIDDV GLINNITRVI STDFKVNMRS ITVDTNEGIF DGSIMIFVND TEHLENLIKN
LLKVRGVTGV TRFDA
//