PURR_CROS8
ID PURR_CROS8 Reviewed; 341 AA.
AC A7MFD3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=ESA_02019;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77272.1; -; Genomic_DNA.
DR RefSeq; WP_012124922.1; NC_009778.1.
DR AlphaFoldDB; A7MFD3; -.
DR SMR; A7MFD3; -.
DR EnsemblBacteria; ABU77272; ABU77272; ESA_02019.
DR GeneID; 56730790; -.
DR KEGG; esa:ESA_02019; -.
DR PATRIC; fig|290339.8.peg.1802; -.
DR HOGENOM; CLU_037628_6_2_6; -.
DR OMA; ARWVGPP; -.
DR OrthoDB; 1796334at2; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000000260; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 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 Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 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_1000085870"
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 221
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; 38086 MW; E6197903C34FAE1D CRC64;
MATIKDVAKR ANVSTTTVSH VINKTRFVAE ETRNAVWAAI KELHYSPSAV ARSLKVNHTK
SIGLLATSSE APYFAEIIEA VENSCFAKGY TLILGNAHNN LEKQRAYLSM MAQKRVDGLL
VMCSEYPQPL LSTLEEYRHI PMVVMDWGEA KADFTDSVID NAFQGGYLAG RYLIERGHRD
IGVIPGQLER NTGVGRFSGF MKALEEAAIK VPENWIVQGD FEPESGYRAM QQILSQPQRP
TAVFCGGDIM AMGAICAADE MGLRVPQDIS IIGYDNVRNA RFFSPALTTI HQPKETLGQT
AFNMLLDRIV NKREESQTIE VHPRLIERRS VADGPFRDYR R
