MODE_HAEIN
ID MODE_HAEIN Reviewed; 255 AA.
AC P45324; Q9R7E9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcriptional regulator ModE;
GN Name=modE; OrderedLocusNames=HI_1694;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2;
RA McLaughlin R., Abu K.Y., Young R., Spinola S., Apicella M.A.;
RT "Characterization and sequence of the lsg locus from Haemophilus
RT influenzae.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP REVIEW.
RX PubMed=9325422; DOI=10.1007/s002030050508;
RA Grunden A.M., Shanmugam K.T.;
RT "Molybdate transport and regulation in bacteria.";
RL Arch. Microbiol. 168:345-354(1997).
CC -!- FUNCTION: The ModE-Mo complex acts as a repressor of the modABC operon,
CC involved in the transport of molybdate. Upon binding molybdate, the
CC conformation of the protein changes, promoting dimerization of ModE-Mo.
CC The protein dimer is then competent to bind a DNA region, upstream of
CC the modABC operon. Acts also as an enhancer of the expression of genes
CC coding for molybdoenzymes, both directly and indirectly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ModE family. {ECO:0000305}.
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DR EMBL; M94855; AAA24984.1; -; Genomic_DNA.
DR EMBL; L42023; AAC23340.1; -; Genomic_DNA.
DR PIR; B64175; B64175.
DR RefSeq; NP_439836.1; NC_000907.1.
DR RefSeq; WP_005694183.1; NC_000907.1.
DR AlphaFoldDB; P45324; -.
DR SMR; P45324; -.
DR STRING; 71421.HI_1694; -.
DR EnsemblBacteria; AAC23340; AAC23340; HI_1694.
DR KEGG; hin:HI_1694; -.
DR PATRIC; fig|71421.8.peg.1773; -.
DR eggNOG; COG2005; Bacteria.
DR HOGENOM; CLU_087839_0_0_6; -.
DR OMA; RTSMRNQ; -.
DR PhylomeDB; P45324; -.
DR BioCyc; HINF71421:G1GJ1-1710-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR016462; ModE.
DR InterPro; IPR003725; ModE-bd_N.
DR InterPro; IPR004606; Mop_domain.
DR InterPro; IPR005116; Transp-assoc_OB_typ1.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03459; TOBE; 1.
DR PIRSF; PIRSF005763; Txn_reg_ModE; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR TIGRFAMs; TIGR00637; ModE_repress; 1.
DR TIGRFAMs; TIGR00638; Mop; 1.
DR PROSITE; PS51866; MOP; 2.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Molybdenum; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transport.
FT CHAIN 1..255
FT /note="Transcriptional regulator ModE"
FT /id="PRO_0000201127"
FT DOMAIN 124..191
FT /note="Mop 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT DOMAIN 194..253
FT /note="Mop 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT DNA_BIND 34..80
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..121
FT /note="I"
FT REGION 125..133
FT /note="Required for dimer formation and molybdate binding"
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="A -> V (in Ref. 1; AAA24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> E (in Ref. 1; AAA24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="P -> S (in Ref. 1; AAA24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="E -> G (in Ref. 1; AAA24984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28898 MW; FA5B7D025E9EB271 CRC64;
MKNTEILLTI KLQQALFIDP KRVRLLKEIQ QCGSINQAAK NAKVSYKSAW DHLEAMNKIS
PRPLLERNTG GKNGGGTALT TYAERLLQLY DLLERTQEHA FHILQDESVP LDSLLTATAR
FSLQSSARNQ FFGRVAQQRI IDSRCVVDVN VQGLPTPLQV SITTKSSARL KLITEKEVML
MFKAPWVKIS EQPLANQPNQ FPVNIKSLNE EEAILQFAES NIEFCATVHQ PNQWQIEQQV
WIHIDQEQII LATLG
