ID A0A1B6YEF4_9BACT Unreviewed; 747 AA.
AC A0A1B6YEF4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:OAN64716.1};
GN ORFNames=A8B79_00810 {ECO:0000313|EMBL:OAN64716.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN64716.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN64716.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN64716.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN64716.1}.
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DR EMBL; LXYG01000001; OAN64716.1; -; Genomic_DNA.
DR RefSeq; WP_066216728.1; NZ_LXYG01000001.1.
DR AlphaFoldDB; A0A1B6YEF4; -.
DR STRING; 1849360.A8B79_00810; -.
DR InParanoid; A0A1B6YEF4; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000078514; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000078514}.
FT DOMAIN 409..470
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT COILED 18..45
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 747 AA; 86059 MW; 0BEED2465DFDA7D2 CRC64;
MSDLKEIART DLESLKLKKA QKQDLKQLLE ECREFIGEIN EEQVEKAFKL CYLSHDGMVR
ASGEPYYYHP VEVAKIVARE INIDEISVIA ALLHDTVEDT SVTLEDIEYW FGKEVAVIIN
GVTKIEGVFK SRDSKQAETF MKLLLSMAED IRVVLIKFAD RLHNMRTIHH LKREKQMKIA
NETMDLYAPL AHRFGLFKIK NELEDLCFKT LDPTSFKFVA RKLKEKKESR EKFIKQFMTP
VEKQLKELKL NFEIKGRPKH IYSIYKKMQR QQKPFEEIYD LFAIRVILGE PHSKEDCWRV
YSIFTDWYTP IPERFRDFIS VPKANGYQSL HTTVITNQGK KVEVQIRTRK MDDIAEKGLA
AHWKYKEGAQ EGSESLDKFV NWVRDVLDNP RPDAATDFVK DFQLNLYQEE LYVFTPKGEL
TTLPNGATAI DFAFDIHSEV GERAMAAKVN GKMVPLRQKL SNGDQVEILT GNKINLNVDW
IDDVVTHKAK SRIRQYIKQK ERAVSDEGKA IWDKRIDRGK IEISDQELTK FAKMYDFTTT
QDMFYAIGVG SFDVNKLFGE VKKYKSTGRI EEEQSESTKA TEDEIQQKYI KEARSVGDGK
SLIINGELSN VKYSYANCCN PIPGDDVIGF ISRTGDIKIH RSMCNNALHL IKTEGERIVD
VDWSKNIETK FLGAVKVIGE DRVGMINDIT DVLSKSLSTN MKSINVNSDS GMFEGIISLY
VDGLSHLKKI MKRLERVEGV KNVLRYE
//