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Entry: A0A0F0XT72_9ENTR
LinkDB: A0A0F0XT72_9ENTR
Original site: A0A0F0XT72_9ENTR 
ID   A0A0F0XT72_9ENTR        Unreviewed;       341 AA.
AC   A0A0F0XT72; A0A0H0CS33;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   ECO:0000313|EMBL:BBW21525.1};
GN   ORFNames=B9Q37_10945 {ECO:0000313|EMBL:PJD76048.1}, DP199_09715
GN   {ECO:0000313|EMBL:RAY73384.1}, STN0717ENT53_18600
GN   {ECO:0000313|EMBL:BBW21525.1};
OS   Enterobacter kobei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=208224 {ECO:0000313|EMBL:RAY73384.1, ECO:0000313|Proteomes:UP000250452};
RN   [1] {ECO:0000313|EMBL:PJD76048.1, ECO:0000313|Proteomes:UP000230495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ECC1097 {ECO:0000313|EMBL:PJD76048.1};
RX   PubMed=29088362;
RA   Zhou K., Yu W., Cao X., Shen P., Lu H., Luo Q., Rossen J.W.A., Xiao Y.;
RT   "Characterization of the population structure, drug resistance mechanisms
RT   and plasmids of the community-associated Enterobacter cloacae complex in
RT   China.";
RL   J. Antimicrob. Chemother. 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:RAY73384.1, ECO:0000313|Proteomes:UP000250452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=131G4 {ECO:0000313|EMBL:RAY73384.1,
RC   ECO:0000313|Proteomes:UP000250452};
RA   Jousset A.B., Oueslati S., Bernabeu S., Takissian J., Creton E., Vogel A.,
RA   Cotellon G., Bonnin R.A., Dortet L., Naas T.;
RT   "ACT-28, a chromosomally-encoded AmpC with carbapenemase activity from
RT   Enterobacter kobei.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BBW21525.1, ECO:0000313|Proteomes:UP000594062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STN0717-53 {ECO:0000313|EMBL:BBW21525.1,
RC   ECO:0000313|Proteomes:UP000594062};
RA   Sekizuka T., Katagiri M., Asai K., Kuroda M.;
RT   "complete genome sequences of Enterobacter kobei str. STN0717-53 isolated
RT   from hospital sewage.";
RL   Submitted (FEB-2020) 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}.
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DR   EMBL; AP022498; BBW21525.1; -; Genomic_DNA.
DR   EMBL; NEEU01000003; PJD76048.1; -; Genomic_DNA.
DR   EMBL; QMCU01000031; RAY73384.1; -; Genomic_DNA.
DR   RefSeq; WP_014883552.1; NZ_VTUD01000020.1.
DR   STRING; 208224.BH713_09375; -.
DR   GeneID; 72831781; -.
DR   KEGG; ekb:BFV64_09630; -.
DR   KEGG; eno:ECENHK_09515; -.
DR   OrthoDB; 9798934at2; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000230495; Unassembled WGS sequence.
DR   Proteomes; UP000250452; Unassembled WGS sequence.
DR   Proteomes; UP000594062; Chromosome.
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:SF142; HTH-TYPE TRANSCRIPTIONAL REPRESSOR PURR-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};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, 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   341 AA;  38139 MW;  EAFEAB53957385EB CRC64;
     MATIKDVAKR ANVSTTTVSH VINKTRFVAE ETRNAVWAAI KELHYSPSAV ARSLKVNHTK
     SIGLLATSSE AAYFAEIIEA VEKNCFQKGY TLILGNAWNS IEKQRAYLSM MAQKRVDGLL
     VMCSEYPESV LSMLEEYRHI PMVVMDWGEA RADFTDSVID NAFEGGYMAG RYLIERGHRE
     IGVIPGPLER NTGAGRLAGF MKAMEEALIT VPENWIVQGD FEPESGYRAM QQIVSQQHRP
     TAVFCGGDIM AMGALCAADE LGLRVPQDIS VIGYDNVRNA RFFTPALTTI HQPKDSLGET
     AFNMLLDRIV NKREESQSIE VHPRLIERRS VADGPFRDYR R
//
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