MALI_ECOLI
ID MALI_ECOLI Reviewed; 342 AA.
AC P18811; P77151;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Maltose regulon regulatory protein MalI;
GN Name=malI; OrderedLocusNames=b1620, JW1612;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2670898; DOI=10.1128/jb.171.9.4888-4899.1989;
RA Reidl J., Roemisch K., Ehrmann M., Boos W.;
RT "MalI, a novel protein involved in regulation of the maltose system of
RT Escherichia coli, is highly homologous to the repressor proteins GalR,
RT CytR, and LacI.";
RL J. Bacteriol. 171:4888-4899(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1856179; DOI=10.1128/jb.173.15.4862-4876.1991;
RA Reidl J., Boos W.;
RT "The malX malY operon of Escherichia coli encodes a novel enzyme II of the
RT phosphotransferase system recognizing glucose and maltose and an enzyme
RT abolishing the endogenous induction of the maltose system.";
RL J. Bacteriol. 173:4862-4876(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Repressor for the malX and malY genes. Also regulates its own
CC expression. Binds maltose as an inducer. {ECO:0000269|PubMed:1856179}.
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DR EMBL; M28539; AAA24104.1; -; Genomic_DNA.
DR EMBL; M60722; AAA24097.1; -; mRNA.
DR EMBL; U00096; AAC74692.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15371.1; -; Genomic_DNA.
DR PIR; F64918; RPECML.
DR RefSeq; NP_416137.1; NC_000913.3.
DR RefSeq; WP_000179510.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P18811; -.
DR SMR; P18811; -.
DR BioGRID; 4261130; 18.
DR BioGRID; 851439; 3.
DR DIP; DIP-10143N; -.
DR IntAct; P18811; 6.
DR STRING; 511145.b1620; -.
DR PaxDb; P18811; -.
DR PRIDE; P18811; -.
DR EnsemblBacteria; AAC74692; AAC74692; b1620.
DR EnsemblBacteria; BAA15371; BAA15371; BAA15371.
DR GeneID; 947104; -.
DR KEGG; ecj:JW1612; -.
DR KEGG; eco:b1620; -.
DR PATRIC; fig|1411691.4.peg.641; -.
DR EchoBASE; EB0552; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_0_6; -.
DR InParanoid; P18811; -.
DR OMA; DGLIFCS; -.
DR PhylomeDB; P18811; -.
DR BioCyc; EcoCyc:PD00361; -.
DR PRO; PR:P18811; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000930; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..342
FT /note="Maltose regulon regulatory protein MalI"
FT /id="PRO_0000107966"
FT DOMAIN 7..61
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 9..28
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT CONFLICT 287..297
FT /note="FTDATPTTLDD -> IYRCDTNHTCMH (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..342
FT /note="RMMQKITHEETHSRNLIIPARLIAAK -> SHDAKNHP (in Ref. 1
FT and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 36625 MW; F1355C6E37FB2C14 CRC64;
MATAKKITIH DVALAAGVSV STVSLVLSGK GRISTATGER VNAAIEELGF VRNRQASALR
GGQSGVIGLI VRDLSAPFYA ELTAGLTEAL EAQGRMVFLL HGGKDGEQLA QRFSLLLNQG
VDGVVIAGAA GSSDDLRRMA EEKAIPVIFA SRASYLDDVD TVRPDNMQAA QLLTEHLIRN
GHQRIAWLGG QSSSLTRAER VGGYCATLLK FGLPFHSDWV LECTSSQKQA AEAITALLRH
NPTISAVVCY NETIAMGAWF GLLKAGRQSG ESGVDRYFEQ QVSLAAFTDA TPTTLDDIPV
TWASTPAREL GITLADRMMQ KITHEETHSR NLIIPARLIA AK
