ID A0A1Q3RUB9_9FLAO Unreviewed; 739 AA.
AC A0A1Q3RUB9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:OJV67732.1};
GN ORFNames=BGO42_17035 {ECO:0000313|EMBL:OJV67732.1};
OS Flavobacterium sp. 40-81.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1896169 {ECO:0000313|EMBL:OJV67732.1, ECO:0000313|Proteomes:UP000185767};
RN [1] {ECO:0000313|EMBL:OJV67732.1, ECO:0000313|Proteomes:UP000185767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=40-81 {ECO:0000313|EMBL:OJV67732.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJV67732.1}.
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DR EMBL; MKTM01000041; OJV67732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3RUB9; -.
DR STRING; 1896169.BGO42_17035; -.
DR Proteomes; UP000185767; Unassembled WGS sequence.
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; 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;
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 739 AA; 84353 MW; A8DA53EAD1816799 CRC64;
MTEIDLEQEN KAIAREYKEL LRISYQTLTE EDKKLIRKAF DVAVDAHKDQ RRKSGEAYIF
HPIAVAKIVA SEIGLGATSI AAALMHDVVE DTDITVADIE KMFNPKIAKI VDGLTKIAKV
KTDQEISMQA ENFRKMLLTL NDDVRVILIK IADRLHNMQT MESMVDYKQA KIASETLYIY
APLAHRLGLY NIKTQLEDLG LKYTEPDVYM DIVSKMKETK EEQEAYIKSI SEILKKSLDE
EGIEYTMKGR PKSIYSIRRK MLVQGVTFDE VYDKFALRII YRSKPQEEKF LAWKIYSIVT
DHYRPSPSRL RDWISSPKST GYEALHITVM GPKGRWVEIQ VRSERMDEIA EKGYAAHYKY
KQGATEENGL DVWLNQLKEA LENSETNAVD FVEDFKLNLY SKEIYIFTPK GEIKSLPKGA
TSLDFAFSIH SEVGIHTRGT RVNGKLVPLN HVLNSGDQVE IITSPNQKPS PNWLDYVTTS
RARNKIKNVL NESTKKIAED GKELLTRKLR HLKIALNESS INELVNYFKL QTSLDLFYRV
GAGLIDNQQL KDFAAQKNNT LINFFKNKIK RSPNVPSEQI HRNEIIKNYD LLVFGKEQDK
LDYKLSTCCN PIPGDDVFGF ITINEGIKVH RKDCPNAISL QSNFAYRIIP AKWIDSSQEE
FKAVIKITGM DTLGLTNELT KVISNQMHVN IQSIALSGEA GIFNGQVTVV VQNNTILKKL
IDNIKKIDGI EKVTRVHKN
//
