ID A0A0M2K714_9GAMM Unreviewed; 339 AA.
AC A0A0M2K714;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SY86_03645 {ECO:0000313|EMBL:KKF34724.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF34724.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF34724.1, ECO:0000313|Proteomes:UP000033924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF34724.1,
RC ECO:0000313|Proteomes:UP000033924};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKF34724.1}.
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DR EMBL; JXNU01000003; KKF34724.1; -; Genomic_DNA.
DR RefSeq; WP_016169813.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2K714; -.
DR STRING; 65700.SY86_03645; -.
DR PATRIC; fig|65700.7.peg.922; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000033924; Unassembled WGS sequence.
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:UP000033924};
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 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 339 AA; 37400 MW; FA141D3AC28FC0A8 CRC64;
MATIKDVAKH AGVSTTTVSH VINKTRFVAE ETKNAVWAAI KALHYSPSAV ARSLKVNNTK
TIGLLATSSE APYFAEIIEA VENCCFDKGY TLILGNAHNN LQKQQAYLSM MAQKRVDGLL
VMCSEYPDTL IAMLEDNRNI PMVVMDWGEP RGDFTDTVLD NAFEGGYLAG RYLIERGHRD
IGVIPGQMER NTGGGRHAGF LKALAEANIP LSQEWLVQGD FEPESGYQAM QKILSQNERP
TAVFCGGDVM AMGAICAADE MGLRVPQDIS VIGYDNVRNA RYFTPSLTTI HQPKEQLGQT
AFSMLLDRIT SKREESQTIE VYPSLIERRS VADGPFINR
//
