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Database: UniProt
Entry: H0EBI6_9ACTN
LinkDB: H0EBI6_9ACTN
Original site: H0EBI6_9ACTN 
ID   H0EBI6_9ACTN            Unreviewed;       369 AA.
AC   H0EBI6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   03-MAY-2023, entry version 58.
DE   RecName: Full=Redox-sensing transcriptional repressor Rex {ECO:0000256|HAMAP-Rule:MF_01131};
GN   Name=rex {ECO:0000256|HAMAP-Rule:MF_01131};
GN   ORFNames=PAI11_42170 {ECO:0000313|EMBL:EHN08967.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN08967.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN08967.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN08967.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
CC   -!- FUNCTION: Modulates transcription in response to changes in cellular
CC       NADH/NAD(+) redox state. {ECO:0000256|HAMAP-Rule:MF_01131}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01131}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01131}.
CC   -!- SIMILARITY: Belongs to the transcriptional regulatory Rex family.
CC       {ECO:0000256|HAMAP-Rule:MF_01131}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHN08967.1}.
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DR   EMBL; AGUD01000308; EHN08967.1; -; Genomic_DNA.
DR   RefSeq; WP_007578992.1; NZ_AGUD01000308.1.
DR   AlphaFoldDB; H0EBI6; -.
DR   PATRIC; fig|1097667.3.peg.4182; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0051775; P:response to redox state; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01131; Rex; 1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR008554; Glutaredoxin-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009718; Rex_DNA-bd_C_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR022876; Tscrpt_rep_Rex.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR35786; REDOX-SENSING TRANSCRIPTIONAL REPRESSOR REX; 1.
DR   PANTHER; PTHR35786:SF1; REDOX-SENSING TRANSCRIPTIONAL REPRESSOR REX 1; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF05768; Glrx-like; 1.
DR   Pfam; PF06971; Put_DNA-bind_N; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01131};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01131}; NAD {ECO:0000256|HAMAP-Rule:MF_01131};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_01131};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01131};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01131}.
FT   DOMAIN          241..342
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   DNA_BIND        178..217
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01131"
FT   BINDING         252..257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01131"
SQ   SEQUENCE   369 AA;  39210 MW;  79983DF7DB429EB1 CRC64;
     MSAPEVVVFL RPGCHLCADA LDDLDALRAQ EPFTVRTVDI ERDDRLHARY LERIPVIAVA
     GEELCDFAVD SERVLTAVRD LRERLATASG GARAAAASRP AATPAPAAAA VTARPPERRL
     EAVPPEPAVP AVAPRRIVAQ PMSTLDATPA AALDPDEPAA DPVPEVRLGV GQAERLSRYL
     QVLTQARKMG RATMSSQELS AHTHVNSTQI RRDLSGFGRF GKRGVGYDVE ELVTKIRGIL
     HTSQHVGIVL LGAGHLGRAI AGSDVFGDHG FEIVAVLDND PAKIGTPIGD LPIGDVRHLG
     EVVREHEVVV GVIASPAKAA QGLADELVEA GVQIIFNYSG SLLRTPAEVT VHTSSPAVDL
     LHALYYYLA
//
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