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P02920

- LACY_ECOLI

UniProt

P02920 - LACY_ECOLI

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Protein
Lactose permease
Gene
lacY, b0343, JW0334
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 binding Source: EcoliWiki
  2. lactose:proton symporter activity Source: CACAO
  3. sugar:proton symporter activity Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77Cytoplasmic4 Publications
Transmembranei8 – 3427Helical; Name=1
Add
BLAST
Topological domaini35 – 417Periplasmic4 Publications
Transmembranei42 – 7029Helical; Name=2
Add
BLAST
Topological domaini71 – 744Cytoplasmic4 Publications
Transmembranei75 – 10026Helical; Name=3
Add
BLAST
Topological domaini101 – 1044Periplasmic4 Publications
Transmembranei105 – 12925Helical; Name=4
Add
BLAST
Topological domaini130 – 14011Cytoplasmic4 Publications
Add
BLAST
Transmembranei141 – 16323Helical; Name=5
Add
BLAST
Topological domaini164 – 1663Periplasmic4 Publications
Transmembranei167 – 18620Helical; Name=6
Add
BLAST
Topological domaini187 – 22034Cytoplasmic4 Publications
Add
BLAST
Transmembranei221 – 24929Helical; Name=7
Add
BLAST
Topological domaini250 – 2534Periplasmic4 Publications
Transmembranei254 – 27825Helical; Name=8
Add
BLAST
Topological domaini279 – 28810Cytoplasmic4 Publications
Transmembranei289 – 30820Helical; Name=9
Add
BLAST
Topological domaini309 – 3113Periplasmic4 Publications
Transmembranei312 – 33423Helical; Name=10
Add
BLAST
Topological domaini335 – 34612Cytoplasmic4 Publications
Add
BLAST
Transmembranei347 – 37428Helical; Name=11
Add
BLAST
Topological domaini375 – 3773Periplasmic4 Publications
Transmembranei378 – 39821Helical; Name=12
Add
BLAST
Topological domaini399 – 41719Cytoplasmic4 Publications
Add
BLAST

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
Complete GO annotation...

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 permease
PRO_0000196184Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiP02920.

Family & Domainsi

Sequence similaritiesi

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 141 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

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