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Database: UniProt
Entry: A0A0E3ZFN3_9BACT
LinkDB: A0A0E3ZFN3_9BACT
Original site: A0A0E3ZFN3_9BACT 
ID   A0A0E3ZFN3_9BACT        Unreviewed;       730 AA.
AC   A0A0E3ZFN3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=MFS transporter {ECO:0000313|EMBL:AKD03585.1};
GN   ORFNames=PKOR_11140 {ECO:0000313|EMBL:AKD03585.1};
OS   Pontibacter korlensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD03585.1, ECO:0000313|Proteomes:UP000033109};
RN   [1] {ECO:0000313|EMBL:AKD03585.1, ECO:0000313|Proteomes:UP000033109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14-1T {ECO:0000313|EMBL:AKD03585.1,
RC   ECO:0000313|Proteomes:UP000033109};
RX   PubMed=26057562; DOI=10.1038/srep10929;
RA   Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA   Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT   "Unraveling adaptation of Pontibacter korlensis to radiation and
RT   infertility in desert through complete genome and comparative
RT   transcriptomic analysis.";
RL   Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD03585.1; -; Genomic_DNA.
DR   RefSeq; WP_046310796.1; NZ_CP009621.1.
DR   AlphaFoldDB; A0A0E3ZFN3; -.
DR   STRING; 400092.PKOR_11140; -.
DR   KEGG; pko:PKOR_11140; -.
DR   PATRIC; fig|400092.3.peg.2429; -.
DR   HOGENOM; CLU_012300_3_2_10; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000033109; 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:UP000033109}.
FT   DOMAIN          56..155
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          401..462
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   730 AA;  83870 MW;  A6265E1CF7FE6123 CRC64;
     MIDLEAERKE ILRHYRRLLR HAKPFLKDND AKIIKKAFNT SLEAHKDMRR KSGEPYILHP
     LAVAQIAVEE IGLGTTSIVA ALLHDVVEDT ELETADIERE FGPSVAKIIE GLTKISGVFD
     YGTSQQAENF RKMLLTLSDD VRVILIKLAD RLHNMRTLGS MPRHKQLKIA SETMYLYAPL
     AHRLGLYAIK SELEDLYLKY TDTDTYKDIS RKVRQTRSAR NKFIKDFIHP IEDELRKYGF
     KFNIKGRPKS IYSILKKIKK QNITFDEIYD LFAIRIILDV PLENEKAACW QVYSIITDFY
     QPNPDRLRDW VNTPKANGYE SLHTTVMSKS GQWVEVQIRT RRMDEIAERG YAAHWKYKTE
     GAASAESGLE QWINKVRDML ENNTANALEF MDEFRKNLFV EEVFVFTPKG ELIILPDKST
     ALDFAFEIHS QIGLHCLGAK VNQKLVPLSY KLKNGDQVEI LTSQKQKPNE EWLQYVVTSK
     ARTRIKDALR EERKNKAEQG KAMLEARMQY IGVADNQQNL NKLQAFFNVA TLQDLYYRIA
     TGHIDIKNIK EVIFTAAADK VASMLDPKSF DREVQKIRGV TSDMLVIGES TDNWDYKMSK
     CCNPIPGDDV FGFQTEEDGI EIHRTNCKRG IELMSNYGNR IIKAKWTEQK ELAFLAGIRI
     KGTDRVGLVN DLTKVISTSL KVNMRSITID SNDGIFEGNI MVFVNNTGHL DKLIQRMSKV
     NGILSVERFD
//
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