MLC_ECOLI
ID MLC_ECOLI Reviewed; 406 AA.
AC P50456; P77593;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein mlc;
DE AltName: Full=Making large colonies protein;
GN Name=mlc; OrderedLocusNames=b1594, JW1586;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7766024; DOI=10.1271/bbb.59.256;
RA Hosono K., Kakuda H., Ichihara S.;
RT "Decreasing accumulation of acetate in a rich medium by Escherichia coli on
RT introduction of genes on a multicopy plasmid.";
RL Biosci. Biotechnol. Biochem. 59:256-261(1995).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP FUNCTION.
RX PubMed=10464268; DOI=10.1074/jbc.274.36.25398;
RA Kim S.-Y., Nam T.-W., Shin D., Koo B.-M., Seok Y.-J., Ryu S.;
RT "Purification of Mlc and analysis of its effects on the PTS expression in
RT Escherichia coli.";
RL J. Biol. Chem. 274:25398-25402(1999).
RN [6]
RP FUNCTION.
RX PubMed=11361067;
RA Plumbridge J.;
RT "Regulation of PTS gene expression by the homologous transcriptional
RT regulators, Mlc and NagC, in Escherichia coli (or how two similar
RT repressors can behave differently).";
RL J. Mol. Microbiol. Biotechnol. 3:371-380(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS,
RP MUTAGENESIS OF CYS-257 AND CYS-259, AND SUBUNIT.
RX PubMed=15929984; DOI=10.1074/jbc.m504215200;
RA Schiefner A., Gerber K., Seitz S., Welte W., Diederichs K., Boos W.;
RT "The crystal structure of Mlc, a global regulator of sugar metabolism in
RT Escherichia coli.";
RL J. Biol. Chem. 280:29073-29079(2005).
CC -!- FUNCTION: Transcriptional repressor that regulates the expression of
CC proteins that are part of the phosphotransferase system for sugar
CC uptake. Regulates the expression of malT. {ECO:0000269|PubMed:10464268,
CC ECO:0000269|PubMed:11361067}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15929984}.
CC -!- INTERACTION:
CC P50456; P50456: mlc; NbExp=2; IntAct=EBI-1116104, EBI-1116104;
CC P50456; P76346: mtfA; NbExp=2; IntAct=EBI-1116104, EBI-1126682;
CC P50456; P69786: ptsG; NbExp=3; IntAct=EBI-1116104, EBI-903497;
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; D32222; BAA06978.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74666.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15318.1; -; Genomic_DNA.
DR PIR; D64915; D64915.
DR RefSeq; NP_416111.1; NC_000913.3.
DR RefSeq; WP_000225262.1; NZ_SSZK01000001.1.
DR PDB; 1Z6R; X-ray; 2.70 A; A/B/C/D=1-406.
DR PDB; 3BP8; X-ray; 2.85 A; A/B=1-406.
DR PDBsum; 1Z6R; -.
DR PDBsum; 3BP8; -.
DR AlphaFoldDB; P50456; -.
DR SMR; P50456; -.
DR BioGRID; 4259119; 23.
DR ComplexPortal; CPX-2242; mlc-EIIB transcriptional regulator complex.
DR DIP; DIP-10219N; -.
DR IntAct; P50456; 9.
DR STRING; 511145.b1594; -.
DR jPOST; P50456; -.
DR PaxDb; P50456; -.
DR PRIDE; P50456; -.
DR EnsemblBacteria; AAC74666; AAC74666; b1594.
DR EnsemblBacteria; BAA15318; BAA15318; BAA15318.
DR GeneID; 945510; -.
DR KEGG; ecj:JW1586; -.
DR KEGG; eco:b1594; -.
DR PATRIC; fig|1411691.4.peg.668; -.
DR EchoBASE; EB2950; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_13_1_6; -.
DR InParanoid; P50456; -.
DR OMA; FFIRHQQ; -.
DR PhylomeDB; P50456; -.
DR BioCyc; EcoCyc:PD01896; -.
DR EvolutionaryTrace; P50456; -.
DR PRO; PR:P50456; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; TAS:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; DNA-binding; Metal-binding;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..406
FT /note="Protein mlc"
FT /id="PRO_0000095690"
FT DNA_BIND 33..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 257
FT /note="C->A,S: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15929984"
FT MUTAGEN 259
FT /note="C->A,S: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15929984"
FT CONFLICT 179
FT /note="G -> A (in Ref. 1; BAA06978)"
FT /evidence="ECO:0000305"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 213..230
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 309..333
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:1Z6R"
SQ SEQUENCE 406 AA; 44316 MW; 423608797FC980CB CRC64;
MVAENQPGHI DQIKQTNAGA VYRLIDQLGP VSRIDLSRLA QLAPASITKI VREMLEAHLV
QELEIKEAGN RGRPAVGLVV ETEAWHYLSL RISRGEIFLA LRDLSSKLVV EESQELALKD
DLPLLDRIIS HIDQFFIRHQ KKLERLTSIA ITLPGIIDTE NGIVHRMPFY EDVKEMPLGE
ALEQHTGVPV YIQHDISAWT MAEALFGASR GARDVIQVVI DHNVGAGVIT DGHLLHAGSS
SLVEIGHTQV DPYGKRCYCG NHGCLETIAS VDSILELAQL RLNQSMSSML HGQPLTVDSL
CQAALRGDLL AKDIITGVGA HVGRILAIMV NLFNPQKILI GSPLSKAADI LFPVISDSIR
QQALPAYSQH ISVESTQFSN QGTMAGAALV KDAMYNGSLL IRLLQG
