ID A0A2K8XM80_9FLAO Unreviewed; 740 AA.
AC A0A2K8XM80;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:AUC84059.1};
GN ORFNames=CW731_01580 {ECO:0000313|EMBL:AUC84059.1};
OS Polaribacter sp. ALD11.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2058137 {ECO:0000313|EMBL:AUC84059.1, ECO:0000313|Proteomes:UP000232878};
RN [1] {ECO:0000313|EMBL:AUC84059.1, ECO:0000313|Proteomes:UP000232878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALD11 {ECO:0000313|EMBL:AUC84059.1,
RC ECO:0000313|Proteomes:UP000232878};
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}.
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DR EMBL; CP025119; AUC84059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8XM80; -.
DR KEGG; poa:CW731_01580; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000232878; 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:UP000232878}.
FT DOMAIN 59..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 740 AA; 84333 MW; E3621DF6A081CC91 CRC64;
MQYTATIEEE NKEIASRYKH LLKGTYEILS VEDKKLIRKA FEIAVDAHSE QRRKTGEPYI
FHPIAVAKIV ATEIGLGATS IAAALLHDVV EDTDYTIDDM EQLFGETIAR IVNGLTKISR
LNKEQDVSIQ AENFRKMLLT LNDDVRVILI KIADRLHNMQ TMDAMPAYKQ VKIASETLYI
YAPLAHRLGL YNIKTELEDL GLKYTEPEVF NDIVTKIKES KEDQKKYLET FAETLKKGLD
KENFTYDIKG RFKSIYSIRR KMRKQNVTFE EVYDKYAIRI IYTPTSGDDK FDAWKIYTIV
TDYFKPNPTR LRDWISQPKS TGYEALHITV IGPSAQWVEV QIRSSRMNEI AEKGYAAHFK
YKQGNSNESG LETWLNKLKE SLENQSLNAV DFVEEFKLNL YAKEIYVFTP KGDLKSLPKD
ASALDFAFSI HTDVGLKCRG AKVNGKLVPL SHTLKSGDQI EVITTSTNKP NSRWLDFVIT
ARAKTKIRAA LKDEEKKIAE EGKAILTRKL RHLKIPFNEK TINELVSFFK IRTSFDLFYR
IGSGAIDNTN LKTYVAQRNS TILNFFKTKL RRTPSGNKEI VESDEVTSKY DALVFGKEEE
KLDYKLSKCC NPIPGDSVFG FLTINEGIKV HKKNCPNAIS LQSNYAYRIM LAKWIDSTKQ
DFKVFLLISG VDNRGIINDL TKIISSNMGV FINSINIAGN EGVFEGKISL SVKNSSQLNK
LIKSIQKVEG VKKVDRVNSL
//