ID D3V1S6_XENBS Unreviewed; 341 AA.
AC D3V1S6;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=HTH-type transcriptional repressor PurR {ECO:0000256|HAMAP-Rule:MF_01277};
DE AltName: Full=Pur regulon repressor {ECO:0000256|HAMAP-Rule:MF_01277};
DE AltName: Full=Purine nucleotide synthesis repressor {ECO:0000256|HAMAP-Rule:MF_01277};
GN Name=purR {ECO:0000256|HAMAP-Rule:MF_01277,
GN ECO:0000313|EMBL:CBJ81620.1};
GN OrderedLocusNames=XBJ1_2496 {ECO:0000313|EMBL:CBJ81620.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ81620.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ81620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ81620.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
CC -!- FUNCTION: Is the main repressor of the genes involved in the de novo
CC synthesis of purine nucleotides, regulating purB, purC, purEK, purF,
CC purHD, purL, purMN and guaBA expression. PurR is allosterically
CC activated to bind its cognate DNA by binding the purine corepressors,
CC hypoxanthine or guanine, thereby effecting transcription repression.
CC {ECO:0000256|HAMAP-Rule:MF_01277}.
CC -!- PATHWAY: Purine metabolism; purine nucleotide biosynthesis
CC [regulation]. {ECO:0000256|ARBA:ARBA00004693, ECO:0000256|HAMAP-
CC Rule:MF_01277}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01277}.
CC -!- DOMAIN: Consists of two structural and functional domains: an N-
CC terminal DNA-binding domain, approximately the first 60 residues, and a
CC larger C-terminal domain, approximately 280 residues, which imparts the
CC function of corepressor binding and oligomerization.
CC {ECO:0000256|HAMAP-Rule:MF_01277}.
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DR EMBL; FN667741; CBJ81620.1; -; Genomic_DNA.
DR RefSeq; WP_012988924.1; NC_013892.1.
DR AlphaFoldDB; D3V1S6; -.
DR STRING; 406818.XBJ1_2496; -.
DR KEGG; xbo:XBJ1_2496; -.
DR PATRIC; fig|406818.4.peg.2246; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000002045; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01392; HTH_LacI; 1.
DR CDD; cd06275; PBP1_PurR; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR HAMAP; MF_01277; HTH_type_PurR; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR023588; Tscrpt_reg_HTH_PurR.
DR PANTHER; PTHR30146:SF152; HTH-TYPE TRANSCRIPTIONAL REGULATOR EBGR-RELATED; 1.
DR PANTHER; PTHR30146; LACI-RELATED TRANSCRIPTIONAL REPRESSOR; 1.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01277};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01277}; Repressor {ECO:0000256|HAMAP-Rule:MF_01277};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01277};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01277}.
FT DOMAIN 2..56
FT /note="HTH lacI-type"
FT /evidence="ECO:0000259|PROSITE:PS50932"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT DNA_BIND 48..56
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 73
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 190
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 192
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 221
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 275
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
SQ SEQUENCE 341 AA; 38143 MW; E34FCC472B664994 CRC64;
MATIKDVAKR AGVSTTTVSH VINKTRFVAE DTKIAVWAAI KELNYSPSAV ARSLKVNHTK
SIGLLATSSE APYFAEIIES VENSCYSKGY TLILCNSHNN LDKQKAYLAM LAQKRVDGLL
VMCSEYPEQL LGMLEDYRNI PMVVMDWGES RGDFTDAIID NAFHGGYLAG RYLIERGHRD
IASIPGPLAR NTGGGRHQGF LKALKEANID IRNEWIVQGD FEPESGYQAM YQILNQKHRP
TAVFCGGDVM AMGAICAADE LGLRVPQDIS IIGYDNIRNA RYFTPALTTI HQPKERLGQM
AFSMLLDRII NKRENVQTIE VHPRLVERRS VTDGPFIDYR R
//
