ID A0A0C5WBH0_9GAMM Unreviewed; 334 AA.
AC A0A0C5WBH0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=H744_2c2303 {ECO:0000313|EMBL:AJR08966.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR08966.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR08966.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR08966.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01277}.
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DR EMBL; CP005974; AJR08966.1; -; Genomic_DNA.
DR RefSeq; WP_044623553.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WBH0; -.
DR STRING; 658445.H744_2c2303; -.
DR KEGG; pgb:H744_2c2303; -.
DR PATRIC; fig|658445.3.peg.4297; -.
DR HOGENOM; CLU_037628_6_2_6; -.
DR OrthoDB; 9798934at2; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000032303; Chromosome 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000032303};
KW 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 189
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 220
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
FT BINDING 274
FT /ligand="hypoxanthine"
FT /ligand_id="ChEBI:CHEBI:17368"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01277"
SQ SEQUENCE 334 AA; 37313 MW; C2C27E88400AE715 CRC64;
MATIKDVARM AGVSTTTVSH VINKTRFVAE ATQKKVLAAV EELNYAPSAV ARSLKCNTTR
TIGMLVTKST NPFFAEVVHG VEEFCYGAGY TLILCNTEGN LSKQRDYLRM LAEKRVDGLL
VMCSDLDEQL LELLERQKET PMVIMDWGPE SPHTDKIQDN AELGGYVATK FFIEHGHKTI
GCLTGHSEKT ACRERLKGYR KAMAEAGLEV KEEWILEGDF ECESAVAAAK QFIAMEERPT
AIFCFNDIMA MAMISTFQQA GINVPEDISI VGYDNIDLAP YFSPPLTTIH QPKRRLGKSA
VEILMQRVKD KEHAPQVFEM IPELVIRKSV KKLN
//