ID H1LSH2_9FIRM Unreviewed; 226 AA.
AC H1LSH2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HMPREF9099_00400 {ECO:0000313|EMBL:EHO54338.1};
OS Lachnospiraceae bacterium oral taxon 082 str. F0431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO54338.1, ECO:0000313|Proteomes:UP000003005};
RN [1] {ECO:0000313|EMBL:EHO54338.1, ECO:0000313|Proteomes:UP000003005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0431 {ECO:0000313|EMBL:EHO54338.1,
RC ECO:0000313|Proteomes:UP000003005};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHO54338.1}.
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DR EMBL; AGRL01000013; EHO54338.1; -; Genomic_DNA.
DR AlphaFoldDB; H1LSH2; -.
DR PATRIC; fig|861454.3.peg.390; -.
DR eggNOG; COG2344; Bacteria.
DR HOGENOM; CLU_061534_1_0_9; -.
DR Proteomes; UP000003005; 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; 3.40.50.720; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009718; Rex_DNA-bd_C_dom.
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.
DR Pfam; PF02629; CoA_binding; 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; 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};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01131};
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 87..188
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT DNA_BIND 24..63
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01131"
FT BINDING 98..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01131"
SQ SEQUENCE 226 AA; 25694 MW; 329D8E69EEAC772E CRC64;
MHSLDGDIME ERKISRAVIS RLPRYYRYLG ELSEEGVERI SSKELSERMK VTASQIRQDL
NNFGGFGQQG YGYNVRYLYN EIAKILGIDR QHNIIIIGAG HLGQAIANYA NFERRGFLIQ
AMFDVDPNLF GKTVRGARVY SLDSLEKFIS ENDIQIAALT IPKARAMEVA DRLVKSGIKA
IWNFAHIDLT VPDDVIVENV HLSESLMRLS YRVSNMDAIP FEGKYD
//
