ID PURR_YERPA Reviewed; 341 AA.
AC Q1C774;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=HTH-type transcriptional repressor PurR {ECO:0000255|HAMAP-Rule:MF_01277};
DE AltName: Full=Pur regulon repressor {ECO:0000255|HAMAP-Rule:MF_01277};
DE AltName: Full=Purine nucleotide synthesis repressor {ECO:0000255|HAMAP-Rule:MF_01277};
GN Name=purR {ECO:0000255|HAMAP-Rule:MF_01277}; OrderedLocusNames=YPA_1732;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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:0000255|HAMAP-Rule:MF_01277}.
CC -!- PATHWAY: Purine metabolism; purine nucleotide biosynthesis
CC [regulation].
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01277}.
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DR EMBL; CP000308; ABG13698.1; -; Genomic_DNA.
DR RefSeq; WP_002220297.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C774; -.
DR SMR; Q1C774; -.
DR KEGG; ypa:YPA_1732; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000001971; 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; Purine biosynthesis; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..341
FT /note="HTH-type transcriptional repressor PurR"
FT /id="PRO_0000279678"
FT DOMAIN 2..56
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT DNA_BIND 48..56
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 73
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 190
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 192
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 275
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
SQ SEQUENCE 341 AA; 37779 MW; 87F4F15C4EF42B49 CRC64;
MATIKDVAKH AGVSTTTVSH VINKTRFVAE NTKAAVWAAI KELHYSPSAV ARSLKVNHTK
SIGLLATSSE APYFAEVIEA VENSCYSKGY TLILCNSHNN LDKQKAYLAM LAQKRVDGLL
VMCSEYPDQL LGMLEDYRNI PMVVMDWGTA RGDFTDSIID NAFEGGYLAG RYLIERGHRD
IGAIPGQLAR NTGGGRHQGF LKALEEANIP VREEWIVQGD SEPESGYKAM HQILTQKHRP
TAVFCGGDIM AMGAICAADE LGLRVPQDIS VIGYDNVRNA RYFSPALTTI HQPKERLGET
AFAMLLDRIV SKREDPQTIE VHPKLVERRS VADGPFRDYR R
//
