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P02920

- LACY_ECOLI

UniProt

P02920 - LACY_ECOLI

Protein

Lactose permease

Gene

lacY

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei126 – 1261Substrate binding
    Sitei144 – 1441Substrate binding
    Sitei269 – 2691Substrate binding and proton translocation
    Sitei302 – 3021Proton translocation
    Sitei322 – 3221Proton translocation
    Sitei325 – 3251Proton translocation

    GO - Molecular functioni

    1. lactose:proton symporter activity Source: CACAO
    2. lactose binding Source: EcoliWiki
    3. sugar:proton symporter activity Source: EcoliWiki

    GO - Biological processi

    1. carbohydrate transport Source: CACAO
    2. lactose transport Source: EcoCyc
    3. proton transport Source: GOC

    Keywords - Biological processi

    Sugar transport, Symport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:LACY-MONOMER.
    ECOL316407:JW0334-MONOMER.
    MetaCyc:LACY-MONOMER.

    Protein family/group databases

    TCDBi2.A.1.5.1. the major facilitator superfamily (mfs).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactose permease
    Alternative name(s):
    Lactose-proton symport
    Gene namesi
    Name:lacY
    Ordered Locus Names:b0343, JW0334
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10526. lacY.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: EcoliWiki
    2. integral component of plasma membrane Source: EcoCyc
    3. membrane Source: EcoliWiki
    4. plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi237 – 2371D → N or G: Defect in melibiose transport.
    Mutagenesisi358 – 3581K → T: Defect in melibiose transport.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Lactose permeasePRO_0000196184Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-formylmethionine; partial1 Publication

    Keywords - PTMi

    Formylation

    Proteomic databases

    PRIDEiP02920.

    Expressioni

    Gene expression databases

    GenevestigatoriP02920.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-10080N.
    STRINGi511145.b0343.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2 – 43
    Helixi7 – 2620
    Turni27 – 293
    Helixi30 – 356
    Turni36 – 383
    Turni42 – 443
    Helixi46 – 6722
    Helixi68 – 703
    Helixi71 – 733
    Helixi75 – 828
    Helixi87 – 937
    Helixi95 – 1006
    Helixi105 – 1084
    Helixi109 – 1113
    Helixi116 – 1194
    Helixi122 – 13615
    Helixi140 – 1434
    Beta strandi144 – 1463
    Turni147 – 1493
    Helixi150 – 16415
    Helixi167 – 1704
    Turni171 – 1799
    Helixi180 – 1834
    Beta strandi193 – 1953
    Beta strandi197 – 2037
    Helixi210 – 2167
    Helixi220 – 24930
    Beta strandi251 – 2533
    Helixi254 – 2574
    Helixi259 – 28628
    Helixi288 – 30619
    Helixi312 – 3187
    Helixi321 – 34020
    Helixi343 – 35412
    Turni355 – 3573
    Helixi358 – 3658
    Helixi367 – 3704
    Helixi372 – 3754
    Helixi377 – 39620
    Beta strandi408 – 4136
    Turni414 – 4163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2Umodel-A1-417[»]
    1PV6X-ray3.50A/B1-417[»]
    1PV7X-ray3.60A/B1-417[»]
    2CFPX-ray3.30A1-417[»]
    2CFQX-ray2.95A1-417[»]
    2V8NX-ray3.60A/B1-417[»]
    2Y5YX-ray3.38A/B1-417[»]
    ProteinModelPortaliP02920.
    SMRiP02920. Positions 1-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02920.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77Cytoplasmic
    Topological domaini35 – 417Periplasmic
    Topological domaini71 – 744Cytoplasmic
    Topological domaini101 – 1044Periplasmic
    Topological domaini130 – 14011CytoplasmicAdd
    BLAST
    Topological domaini164 – 1663Periplasmic
    Topological domaini187 – 22034CytoplasmicAdd
    BLAST
    Topological domaini250 – 2534Periplasmic
    Topological domaini279 – 28810Cytoplasmic
    Topological domaini309 – 3113Periplasmic
    Topological domaini335 – 34612CytoplasmicAdd
    BLAST
    Topological domaini375 – 3773Periplasmic
    Topological domaini399 – 41719CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 3427Helical; Name=1Add
    BLAST
    Transmembranei42 – 7029Helical; Name=2Add
    BLAST
    Transmembranei75 – 10026Helical; Name=3Add
    BLAST
    Transmembranei105 – 12925Helical; Name=4Add
    BLAST
    Transmembranei141 – 16323Helical; Name=5Add
    BLAST
    Transmembranei167 – 18620Helical; Name=6Add
    BLAST
    Transmembranei221 – 24929Helical; Name=7Add
    BLAST
    Transmembranei254 – 27825Helical; Name=8Add
    BLAST
    Transmembranei289 – 30820Helical; Name=9Add
    BLAST
    Transmembranei312 – 33423Helical; Name=10Add
    BLAST
    Transmembranei347 – 37428Helical; Name=11Add
    BLAST
    Transmembranei378 – 39821Helical; Name=12Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LacY/RafB permease family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0477.
    HOGENOMiHOG000114363.
    KOiK02532.
    OMAiIVGCFKY.
    OrthoDBiEOG6KHG2V.
    PhylomeDBiP02920.

    Family and domain databases

    InterProiIPR000576. LacY/RafB_perm_fam.
    IPR018457. LacY/RafB_perm_fam_CS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view]
    PfamiPF01306. LacY_symp. 1 hit.
    [Graphical view]
    PRINTSiPR00174. LACYSMPORT.
    SUPFAMiSSF103473. SSF103473. 1 hit.
    TIGRFAMsiTIGR00882. 2A0105. 1 hit.
    PROSITEiPS00896. LACY_1. 1 hit.
    PS00897. LACY_2. 1 hit.
    PS50850. MFS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P02920-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA    50
    AISLFSLLFQ PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ 100
    YNILVGSIVG GIYLGFCFNA GAPAVEAFIE KVSRRSNFEF GRARMFGCVG 150
    WALCASIVGI MFTINNQFVF WLGSGCALIL AVLLFFAKTD APSSATVANA 200
    VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD QQFANFFTSF 250
    FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS 300
    VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY 350
    LVCFCFFKQL AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL 400
    SGPGPLSLLR RQVNEVA 417
    Length:417
    Mass (Da):46,503
    Last modified:July 21, 1986 - v1
    Checksum:i24A8062F628CDA32
    GO

    Mass spectrometryi

    Molecular mass is 47357 Da from positions 1 - 417. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01636 Genomic DNA. Translation: AAA24054.1.
    V00295 Genomic DNA. Translation: CAA23571.1.
    X56095 Genomic DNA. Translation: CAA39575.1.
    U73857 Genomic DNA. Translation: AAB18067.1.
    U00096 Genomic DNA. Translation: AAC73446.1.
    AP009048 Genomic DNA. Translation: BAE76125.1.
    PIRiA03418. GREC.
    RefSeqiNP_414877.1. NC_000913.3.
    YP_488637.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73446; AAC73446; b0343.
    BAE76125; BAE76125; BAE76125.
    GeneIDi12934191.
    949083.
    KEGGiecj:Y75_p0332.
    eco:b0343.
    PATRICi32115819. VBIEscCol129921_0351.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01636 Genomic DNA. Translation: AAA24054.1 .
    V00295 Genomic DNA. Translation: CAA23571.1 .
    X56095 Genomic DNA. Translation: CAA39575.1 .
    U73857 Genomic DNA. Translation: AAB18067.1 .
    U00096 Genomic DNA. Translation: AAC73446.1 .
    AP009048 Genomic DNA. Translation: BAE76125.1 .
    PIRi A03418. GREC.
    RefSeqi NP_414877.1. NC_000913.3.
    YP_488637.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M2U model - A 1-417 [» ]
    1PV6 X-ray 3.50 A/B 1-417 [» ]
    1PV7 X-ray 3.60 A/B 1-417 [» ]
    2CFP X-ray 3.30 A 1-417 [» ]
    2CFQ X-ray 2.95 A 1-417 [» ]
    2V8N X-ray 3.60 A/B 1-417 [» ]
    2Y5Y X-ray 3.38 A/B 1-417 [» ]
    ProteinModelPortali P02920.
    SMRi P02920. Positions 1-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10080N.
    STRINGi 511145.b0343.

    Protein family/group databases

    TCDBi 2.A.1.5.1. the major facilitator superfamily (mfs).

    Proteomic databases

    PRIDEi P02920.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73446 ; AAC73446 ; b0343 .
    BAE76125 ; BAE76125 ; BAE76125 .
    GeneIDi 12934191.
    949083.
    KEGGi ecj:Y75_p0332.
    eco:b0343.
    PATRICi 32115819. VBIEscCol129921_0351.

    Organism-specific databases

    EchoBASEi EB0521.
    EcoGenei EG10526. lacY.

    Phylogenomic databases

    eggNOGi COG0477.
    HOGENOMi HOG000114363.
    KOi K02532.
    OMAi IVGCFKY.
    OrthoDBi EOG6KHG2V.
    PhylomeDBi P02920.

    Enzyme and pathway databases

    BioCyci EcoCyc:LACY-MONOMER.
    ECOL316407:JW0334-MONOMER.
    MetaCyc:LACY-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02920.
    PROi P02920.

    Gene expression databases

    Genevestigatori P02920.

    Family and domain databases

    InterProi IPR000576. LacY/RafB_perm_fam.
    IPR018457. LacY/RafB_perm_fam_CS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view ]
    Pfami PF01306. LacY_symp. 1 hit.
    [Graphical view ]
    PRINTSi PR00174. LACYSMPORT.
    SUPFAMi SSF103473. SSF103473. 1 hit.
    TIGRFAMsi TIGR00882. 2A0105. 1 hit.
    PROSITEi PS00896. LACY_1. 1 hit.
    PS00897. LACY_2. 1 hit.
    PS50850. MFS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Pastore J.C., Larigan J.D., Consler T.G., Kaback H.R.
      Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology."
      von Heijne G.
      EMBO J. 5:3021-3027(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    7. "lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion."
      Calamia J., Manoil C.
      Proc. Natl. Acad. Sci. U.S.A. 87:4937-4941(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    8. "Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopy."
      Ujwal M.L., Jung H., Bibi E., Manoil C., Altenbach C., Hubbell W.L., Kaback H.R.
      Biochemistry 34:14909-14917(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    9. "The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli."
      King S.C., Hansen C.L., Wilson T.H.
      Biochim. Biophys. Acta 1062:177-186(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    10. "Amino acid substitution in the lactose carrier protein with the use of amber suppressors."
      Huang A.-M., Lee J.-I., King S.C., Wilson T.H.
      J. Bacteriol. 174:5436-5441(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    11. "The lac permease of Escherichia coli: a prototypic energy-transducing membrane protein."
      Kaback H.R.
      Biochim. Biophys. Acta 1018:160-162(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    12. "Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins."
      Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G., Faull K.F., Kaback H.R.
      Proc. Natl. Acad. Sci. U.S.A. 96:10695-10698(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FORMYLATION AT MET-1, MASS SPECTROMETRY.
    13. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: K12 / MG1655 / ATCC 47076.
    14. "Structure and mechanism of the lactose permease of Escherichia coli."
      Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., Iwata S.
      Science 301:610-615(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF MUTANT GLY-154.

    Entry informationi

    Entry nameiLACY_ECOLI
    AccessioniPrimary (citable) accession number: P02920
    Secondary accession number(s): Q2MC81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3