IACR_PSEPU
ID IACR_PSEPU Reviewed; 167 AA.
AC B0FXI7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=HTH-type transcriptional repressor IacR {ECO:0000305};
GN Name=iacR {ECO:0000303|PubMed:18205812};
GN ORFNames=E6B08_12615 {ECO:0000312|EMBL:QCI12147.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1290;
RX PubMed=18205812; DOI=10.1111/j.1574-6941.2008.00436.x;
RA Leveau J.H.J., Gerards S.;
RT "Discovery of a bacterial gene cluster for catabolism of the plant hormone
RT indole 3-acetic acid.";
RL FEMS Microbiol. Ecol. 65:238-250(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1290;
RA Laird T.S., Leveau J.H.J.;
RT "Genome sequence of Pseudomonas putida 1290, an auxin catabolizing
RT strain.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=1290;
RX PubMed=23881445; DOI=10.1007/s10886-013-0324-x;
RA Scott J.C., Greenhut I.V., Leveau J.H.;
RT "Functional characterization of the bacterial iac genes for degradation of
RT the plant hormone indole-3-acetic acid.";
RL J. Chem. Ecol. 39:942-951(2013).
CC -!- FUNCTION: Probably acts as a repressor of iacA expression.
CC {ECO:0000269|PubMed:23881445}.
CC -!- ACTIVITY REGULATION: Exposure to indole-3-acetic acid (IAA) probably
CC relieves the repressor activity. {ECO:0000269|PubMed:23881445}.
CC -!- INDUCTION: Induced in the presence of IAA.
CC {ECO:0000269|PubMed:23881445}.
CC -!- MISCELLANEOUS: Transformation of P.putida KT2440, which cannot degrade
CC IAA, with the iac gene cluster confers the ability to grow on IAA as a
CC sole source of carbon and energy, but not the ability to chemotaxis
CC towards IAA. {ECO:0000269|PubMed:23881445}.
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DR EMBL; EU360594; ABY62764.1; -; Genomic_DNA.
DR EMBL; CP039371; QCI12147.1; -; Genomic_DNA.
DR PDB; 7KUA; X-ray; 1.89 A; A=1-167.
DR PDBsum; 7KUA; -.
DR SMR; B0FXI7; -.
DR EnsemblBacteria; QCI12147; QCI12147; E6B08_12615.
DR Proteomes; UP000298551; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..167
FT /note="HTH-type transcriptional repressor IacR"
FT /id="PRO_0000454115"
FT DOMAIN 30..162
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT DNA_BIND 76..99
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 33..53
FT /evidence="ECO:0007829|PDB:7KUA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:7KUA"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:7KUA"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7KUA"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:7KUA"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:7KUA"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:7KUA"
SQ SEQUENCE 167 AA; 19347 MW; 3AE3ED3FF6EFD5EF CRC64;
MSNAKNTSAA SPARKGHSHH DPASDEFRKE DFPFYWLARV HGRYTQNMER LLKKIDLDVP
RWRVLWILNE NGESSISEIS THAIAKLSTI TKIVYRMKED GLVDTAPSPE DGRVTQVRIT
EVGLQNIERM QEVTRELFQR SFKGLTEAQV QRLNRMLEVV FHNLETL