ID A0A0J1GTP5_9GAMM Unreviewed; 335 AA.
AC A0A0J1GTP5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ABT58_01745 {ECO:0000313|EMBL:KLV02804.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLV02804.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLV02804.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLV02804.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KLV02804.1}.
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DR EMBL; LDOV01000003; KLV02804.1; -; Genomic_DNA.
DR RefSeq; WP_047872640.1; NZ_PYMF01000011.1.
DR AlphaFoldDB; A0A0J1GTP5; -.
DR PATRIC; fig|754436.4.peg.367; -.
DR OrthoDB; 9798934at2; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000036426; 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:UP000036426};
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 335 AA; 37382 MW; 3FABAD25FEC6660A CRC64;
MATIKDVARM AGVSTTTVSH VINKTRFVAE ATQKKVLAAV DELNYAPSAV ARSLKCNTTR
TIGMLVTKST NPFFAEVVHG VEEYLYGEGY TLILCNTEGN LAKQRDYLRM LAEKRVDGLL
VMCSDLDEQL LQLLERQKDL PMVIMDWGPE SPQTDNIQDN AELGGYVATK FFIEHGHKAI
GCLTGHSEKV ACRERLKGFR KAMSEAGLTV NEDWLLEGDF ECESAVKAAE AFIAMKERPT
AIFCFNDIMA MGLISTFQQA GIRVPDDVSI IGYDNIDLAP YFAPPLTTIH QPKRRLGKSA
VEILMQRVKD KTHETQVFEM VPELVIRKSV RDLNN
//
