ACUR_CERS4
ID ACUR_CERS4 Reviewed; 219 AA.
AC Q3J6K8;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Transcriptional regulator AcuR;
GN Name=acuR; OrderedLocusNames=RHOS4_00080; ORFNames=RSP_1435;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=21249136; DOI=10.1371/journal.pone.0015972;
RA Sullivan M.J., Curson A.R., Shearer N., Todd J.D., Green R.T.,
RA Johnston A.W.;
RT "Unusual regulation of a leaderless operon involved in the catabolism of
RT dimethylsulfoniopropionate in Rhodobacter sphaeroides.";
RL PLoS ONE 6:E15972-E15972(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Osipiuk J., Maltseva N., Freeman L., Joachimiak A.;
RT "Crystal structure of regulatory protein TetR from Rhodobacter
RT sphaeroides.";
RL Submitted (DEC-2007) to the PDB data bank.
CC -!- FUNCTION: A transcriptional repressor for its operon. Probably binds to
CC 2 operator sequences in the promoter. {ECO:0000269|PubMed:21249136}.
CC -!- INDUCTION: Strongly induced by acrylate, the operon product (20-fold),
CC and dimethylsulfonioproprionate, the operon substrate (DMSP, 10-fold).
CC Part of the acuR-acuI-dddL operon. {ECO:0000269|PubMed:21249136}.
CC -!- DISRUPTION PHENOTYPE: Loss of repression of its operon.
CC {ECO:0000269|PubMed:21249136}.
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DR EMBL; CP000143; ABA77576.1; -; Genomic_DNA.
DR RefSeq; WP_011336736.1; NZ_CP030271.1.
DR RefSeq; YP_351477.1; NC_007493.2.
DR PDB; 3BRU; X-ray; 2.30 A; A/B=1-219.
DR PDBsum; 3BRU; -.
DR AlphaFoldDB; Q3J6K8; -.
DR SMR; Q3J6K8; -.
DR STRING; 272943.RSP_1435; -.
DR EnsemblBacteria; ABA77576; ABA77576; RSP_1435.
DR KEGG; rsp:RSP_1435; -.
DR PATRIC; fig|272943.9.peg.299; -.
DR eggNOG; COG1309; Bacteria.
DR OMA; HFSNKEV; -.
DR PhylomeDB; Q3J6K8; -.
DR EvolutionaryTrace; Q3J6K8; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR InterPro; IPR011075; TetR_C.
DR Pfam; PF16925; TetR_C_13; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..219
FT /note="Transcriptional regulator AcuR"
FT /id="PRO_0000420619"
FT DOMAIN 26..86
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 49..68
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:3BRU"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 71..94
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:3BRU"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 141..164
FT /evidence="ECO:0007829|PDB:3BRU"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 175..196
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3BRU"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3BRU"
SQ SEQUENCE 219 AA; 24505 MW; 28AEC9B393D8BA38 CRC64;
MPLTDTPPSV PQKPRRGRPR GAPDASLAHQ SLIRAGLEHL TEKGYSSVGV DEILKAARVP
KGSFYHYFRN KADFGLALIE AYDTYFARLL DQAFLDGSLA PLARLRLFTR MAEEGMARHG
FRRGCLVGNL GQEMGALPDD FRAALIGVLE TWQRRTAQLF REAQACGELS ADHDPDALAE
AFWIGWEGAI LRAKLELRPD PLHSFTRTFG RHFVTRTQE
