MOPR_ACIGI
ID MOPR_ACIGI Reviewed; 560 AA.
AC Q43965;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phenol regulator MopR {ECO:0000303|PubMed:9023219};
GN Name=mopR {ECO:0000303|PubMed:9023219};
OS Acinetobacter guillouiae (Acinetobacter genomosp. 11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=106649;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP INDUCTION, AND DOMAIN.
RC STRAIN=ATCC 11171 / DSM 590 / CCUG 2491 / LMG 988 / NCIMB 8250 / CIP 63.46
RC / B94;
RX PubMed=9023219; DOI=10.1128/jb.179.4.1329-1336.1997;
RA Schirmer F., Ehrt S., Hillen W.;
RT "Expression, inducer spectrum, domain structure, and function of MopR, the
RT regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250.";
RL J. Bacteriol. 179:1329-1336(1997).
RN [2] {ECO:0007744|PDB:5KBE, ECO:0007744|PDB:5KBG, ECO:0007744|PDB:5KBH, ECO:0007744|PDB:5KBI}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-229 IN COMPLEX WITH PHENOL AND
RP ZINC, SUBUNIT, DOMAIN, AND MUTAGENESIS OF HIS-106; TRP-134; GLU-178 AND
RP CYS-189.
RC STRAIN=ATCC 11171 / DSM 590 / CCUG 2491 / LMG 988 / NCIMB 8250 / CIP 63.46
RC / B94;
RX PubMed=27362503; DOI=10.1021/acschembio.6b00020;
RA Ray S., Gunzburg M.J., Wilce M., Panjikar S., Anand R.;
RT "Structural basis of selective aromatic pollutant sensing by the effector
RT binding domain of MopR, an NtrC family transcriptional regulator.";
RL ACS Chem. Biol. 11:2357-2365(2016).
CC -!- FUNCTION: Involved in the regulation of the phenol degradation pathway.
CC Activates phenol hydroxylase expression in the presence of phenol.
CC {ECO:0000269|PubMed:9023219}.
CC -!- ACTIVITY REGULATION: Activity is triggered by phenol binding.
CC {ECO:0000269|PubMed:9023219}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27362503}.
CC -!- INDUCTION: Constitutively expressed at a low level from a sigma70-type
CC promoter. {ECO:0000269|PubMed:9023219}.
CC -!- DOMAIN: Contains an N-terminal signal reception (A) domain, followed by
CC a hinge region (B domain), a transcription activation (C) domain and a
CC C-terminal D domain. The A domain directly responds to external
CC signals, the C domain contains the ATP-binding region that provides
CC energy, and the D domain contains a helix-turn-helix DNA binding motif.
CC {ECO:0000305|PubMed:27362503, ECO:0000305|PubMed:9023219}.
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DR EMBL; Z69251; CAA93242.1; -; Genomic_DNA.
DR RefSeq; WP_004721355.1; NZ_VZOG01000030.1.
DR PDB; 5KBE; X-ray; 2.50 A; A/B=1-229.
DR PDB; 5KBG; X-ray; 2.80 A; A/B=1-229.
DR PDB; 5KBH; X-ray; 2.55 A; A/B=1-229.
DR PDB; 5KBI; X-ray; 2.90 A; A/B=1-229.
DR PDB; 6L79; X-ray; 2.20 A; A=1-229.
DR PDBsum; 5KBE; -.
DR PDBsum; 5KBG; -.
DR PDBsum; 5KBH; -.
DR PDBsum; 5KBI; -.
DR PDBsum; 6L79; -.
DR AlphaFoldDB; Q43965; -.
DR SMR; Q43965; -.
DR STRING; 106649.GCA_000829655_03942; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR InterPro; IPR004096; V4R.
DR InterPro; IPR010523; XylR_N.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR Pfam; PF02830; V4R; 1.
DR Pfam; PF06505; XylR_N; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00989; V4R; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; DNA-binding; Metal-binding;
KW Nucleotide-binding; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..560
FT /note="Phenol regulator MopR"
FT /id="PRO_0000438296"
FT DOMAIN 245..474
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 106
FT /ligand="phenol"
FT /ligand_id="ChEBI:CHEBI:15882"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 134
FT /ligand="phenol"
FT /ligand_id="ChEBI:CHEBI:15882"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:27362503"
FT BINDING 273..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 336..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MUTAGEN 106
FT /note="H->A: 17-fold increase in Kd for phenol."
FT /evidence="ECO:0000269|PubMed:27362503"
FT MUTAGEN 134
FT /note="W->A: 6-fold increase in Kd for phenol."
FT /evidence="ECO:0000269|PubMed:27362503"
FT MUTAGEN 178
FT /note="E->A: Exhibits extremely low solubility."
FT /evidence="ECO:0000269|PubMed:27362503"
FT MUTAGEN 189
FT /note="C->A: Exhibits extremely low solubility."
FT /evidence="ECO:0000269|PubMed:27362503"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6L79"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 64..89
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:6L79"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 156..170
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6L79"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:6L79"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:5KBE"
SQ SEQUENCE 560 AA; 63628 MW; 0B149710FFE87241 CRC64;
MSPAKDVKVY KKILEQNKDI QDLLDKIVFD AQHGQIWFDE NRMLLMHTSI LGFLRKDLYQ
MLGLERTKRF FIRCGYQAGM RDAEVTSKLR PNLNEAEAFM AGPQMHGIRG MVQVEVNELH
LSHDLKQFYA DFNWLNSFEA EVHLSEFGAS DQPACWMLLG YACGYSSFVM GQTIIYQETH
CVAQGDEHCR IIGKPLSEWE NADELIRFMS PDAVSDEIIA LQAELNQLKK NIYTEAESDY
TMFNAVGESV AYRKVCDLLK KAAGSKVAVL LQGETGVGKE AFARGIHNGS QRQAQPFVAV
NCACIPPDLI ESELFGVEKG AFTGAVQSRM GKFERAHGGT IFLDEVVELS PRAQAALLRM
LQEGEFERVG DSRTRQVDVR LVAATNEDLE QAVKDGKFRA DLYYRLNIFP VIIPPLRERR
EDIPLLINHF LARFENMYNK TLKGLSDKAK NFMMKYDWPG NIRELENLLE RATLLTDHQQ
EIKLDSLFPQ HKDLEAVGET AQSLINVEDL FSENFSLDQL EQNIIRSAMD KSQQNVSEAA
RMLGISRATL DYRLKKITLG
