PURR_VIBCH
ID PURR_VIBCH Reviewed; 336 AA.
AC Q9KRC1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=VC_1721;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF94871.1; -; Genomic_DNA.
DR PIR; A82165; A82165.
DR RefSeq; NP_231357.1; NC_002505.1.
DR RefSeq; WP_000201014.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRC1; -.
DR SMR; Q9KRC1; -.
DR STRING; 243277.VC_1721; -.
DR DNASU; 2613726; -.
DR EnsemblBacteria; AAF94871; AAF94871; VC_1721.
DR GeneID; 57740373; -.
DR KEGG; vch:VC_1721; -.
DR PATRIC; fig|243277.26.peg.1647; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR OMA; ARWVGPP; -.
DR BioCyc; VCHO:VC1721-MON; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..336
FT /note="HTH-type transcriptional repressor PurR"
FT /id="PRO_0000279672"
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 336 AA; 38002 MW; 0E9461EB51FC727F CRC64;
MATIKDVARL AGVSTTTVSH VINKTRFVAE TTQEKVMEAV KQLNYAPSAV ARSLKCNTTR
TIGMLVTQST NLFFSEVIDG VESYCYRQGY TLILCNTGGI YEKQRDYIRM LAEKRVDGIL
VMCSDLTQEL QDMLDAHKDI PKVVMDWGPE TSHADKIIDN SEEGGYLATK YLTDRGHTEI
ACLSGHFVKA ACQERIQGFR RAMAEAKLTV NEDWILEGNF ECDTAVLAAD KIIAMDKRPT
AVFCFNDTMA LGLMSRLQQK GIRIPEDMSV IGYDNIELAE YFSPPLTTVH QPKRRVGKNA
FEILLERIKD KEHERRIFEM HPEIVERDTV KDLTKS
