ID PURR_VIBPA Reviewed; 334 AA.
AC Q87QW9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=VP1030;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC59293.1; -; Genomic_DNA.
DR RefSeq; NP_797409.1; NC_004603.1.
DR RefSeq; WP_005457245.1; NC_004603.1.
DR AlphaFoldDB; Q87QW9; -.
DR SMR; Q87QW9; -.
DR GeneID; 1188534; -.
DR KEGG; vpa:VP1030; -.
DR PATRIC; fig|223926.6.peg.976; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000002493; Chromosome 1.
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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..334
FT /note="HTH-type transcriptional repressor PurR"
FT /id="PRO_0000279674"
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 189
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 220
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT BINDING 274
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
SQ SEQUENCE 334 AA; 37674 MW; 0BEFE2EAD7609E37 CRC64;
MATIKDVARL AGVSTTTVSH VINKTRFVAE ATQEKVMKAV DELNYAPSAV ARSLKCNSTR
TIGMLVTQST NLFFSEVIDG VESYCYRQGY TLILCNTGGI YEKQRDYIRM LAEKRVDGIL
VMCSDLTEEL KEMLDRHSDI PKVVMDWGPE SSRADKIIDN SEEGGYLATK YLIDNGHTDI
ACLSGHFEKL ACQERIAGFR RAMAEAKLPI NEDWILEGNF ECDTAVLVAD KITAMEKRPT
AVFCFNDTMA LGLMSRLQQN GIKVPDDVSV IGYDNIELAE YFSPPLTTIH QPKRRVGKNA
FEILLERIKD KEHEKRVFEM QPEIVIRNTV KKLN
//
