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P50456 (MLC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein mlc
Alternative name(s):
Making large colonies protein
Gene names
Name:mlc
Ordered Locus Names:b1594, JW1586
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. Regulates the expression of malT. Ref.5 Ref.6

Subunit structure

Homodimer. Ref.7

Sequence similarities

Belongs to the ROK (NagC/XylR) family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mtfAP763462EBI-1116104,EBI-1126682

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Protein mlc
PRO_0000095690

Regions

DNA binding33 – 4210H-T-H motif By similarity

Sites

Metal binding2471Zinc
Metal binding2571Zinc
Metal binding2591Zinc
Metal binding2641Zinc

Experimental info

Mutagenesis2571C → A or S: Strongly reduced activity. Ref.7
Mutagenesis2591C → A or S: Strongly reduced activity. Ref.7
Sequence conflict1791G → A in BAA06978. Ref.1

Secondary structure

.................................................................. 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50456 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 423608797FC980CB

FASTA40644,316
        10         20         30         40         50         60 
MVAENQPGHI DQIKQTNAGA VYRLIDQLGP VSRIDLSRLA QLAPASITKI VREMLEAHLV 

        70         80         90        100        110        120 
QELEIKEAGN RGRPAVGLVV ETEAWHYLSL RISRGEIFLA LRDLSSKLVV EESQELALKD 

       130        140        150        160        170        180 
DLPLLDRIIS HIDQFFIRHQ KKLERLTSIA ITLPGIIDTE NGIVHRMPFY EDVKEMPLGE 

       190        200        210        220        230        240 
ALEQHTGVPV YIQHDISAWT MAEALFGASR GARDVIQVVI DHNVGAGVIT DGHLLHAGSS 

       250        260        270        280        290        300 
SLVEIGHTQV DPYGKRCYCG NHGCLETIAS VDSILELAQL RLNQSMSSML HGQPLTVDSL 

       310        320        330        340        350        360 
CQAALRGDLL AKDIITGVGA HVGRILAIMV NLFNPQKILI GSPLSKAADI LFPVISDSIR 

       370        380        390        400 
QQALPAYSQH ISVESTQFSN QGTMAGAALV KDAMYNGSLL IRLLQG 

« Hide

References

« Hide 'large scale' references
[1]"Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid."
Hosono K., Kakuda H., Ichihara S.
Biosci. Biotechnol. Biochem. 59:256-261(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Purification of Mlc and analysis of its effects on the PTS expression in Escherichia coli."
Kim S.-Y., Nam T.-W., Shin D., Koo B.-M., Seok Y.-J., Ryu S.
J. Biol. Chem. 274:25398-25402(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Regulation of PTS gene expression by the homologous transcriptional regulators, Mlc and NagC, in Escherichia coli (or how two similar repressors can behave differently)."
Plumbridge J.
J. Mol. Microbiol. Biotechnol. 3:371-380(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli."
Schiefner A., Gerber K., Seitz S., Welte W., Diederichs K., Boos W.
J. Biol. Chem. 280:29073-29079(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, MUTAGENESIS OF CYS-257 AND CYS-259, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D32222 Genomic DNA. Translation: BAA06978.1.
U00096 Genomic DNA. Translation: AAC74666.1.
AP009048 Genomic DNA. Translation: BAA15318.1.
PIRD64915.
RefSeqNP_416111.1. NC_000913.2.
YP_489857.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6RX-ray2.70A/B/C/D1-406[»]
3BP8X-ray2.85A/B1-406[»]
ProteinModelPortalP50456.
SMRP50456. Positions 12-406.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10219N.
IntActP50456. 9 interactions.
STRING511145.b1594.

Proteomic databases

PaxDbP50456.
PRIDEP50456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74666; AAC74666; b1594.
BAA15318; BAA15318; BAA15318.
GeneID12930125.
945510.
KEGGecj:Y75_p1570.
eco:b1594.
PATRIC32118490. VBIEscCol129921_1665.

Organism-specific databases

EchoBASEEB2950.
EcoGeneEG13156. mlc.

Phylogenomic databases

eggNOGCOG1940.
HOGENOMHOG000275182.
KOK15545.
OMAPTYSQHI.
ProtClustDBCLSK870201.

Enzyme and pathway databases

BioCycEcoCyc:PD01896.
ECOL316407:JW1586-MONOMER.

Gene expression databases

GenevestigatorP50456.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR000600. ROK.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00480. ROK. 1 hit.
[Graphical view]
PROSITEPS01125. ROK. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50456.

Entry information

Entry nameMLC_ECOLI
AccessionPrimary (citable) accession number: P50456
Secondary accession number(s): P77593
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families