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P02920

- LACY_ECOLI

UniProt

P02920 - LACY_ECOLI

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Protein

Lactose permease

Gene

lacY

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: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
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 – 77Cytoplasmic
Transmembranei8 – 3427Helical; Name=1Add
BLAST
Topological domaini35 – 417Periplasmic
Transmembranei42 – 7029Helical; Name=2Add
BLAST
Topological domaini71 – 744Cytoplasmic
Transmembranei75 – 10026Helical; Name=3Add
BLAST
Topological domaini101 – 1044Periplasmic
Transmembranei105 – 12925Helical; Name=4Add
BLAST
Topological domaini130 – 14011CytoplasmicAdd
BLAST
Transmembranei141 – 16323Helical; Name=5Add
BLAST
Topological domaini164 – 1663Periplasmic
Transmembranei167 – 18620Helical; Name=6Add
BLAST
Topological domaini187 – 22034CytoplasmicAdd
BLAST
Transmembranei221 – 24929Helical; Name=7Add
BLAST
Topological domaini250 – 2534Periplasmic
Transmembranei254 – 27825Helical; Name=8Add
BLAST
Topological domaini279 – 28810Cytoplasmic
Transmembranei289 – 30820Helical; Name=9Add
BLAST
Topological domaini309 – 3113Periplasmic
Transmembranei312 – 33423Helical; Name=10Add
BLAST
Topological domaini335 – 34612CytoplasmicAdd
BLAST
Transmembranei347 – 37428Helical; Name=11Add
BLAST
Topological domaini375 – 3773Periplasmic
Transmembranei378 – 39821Helical; Name=12Add
BLAST
Topological domaini399 – 41719CytoplasmicAdd
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 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 – 43Combined sources
Helixi7 – 2620Combined sources
Turni27 – 293Combined sources
Helixi30 – 356Combined sources
Turni36 – 383Combined sources
Turni42 – 443Combined sources
Helixi46 – 6722Combined sources
Helixi68 – 703Combined sources
Helixi71 – 733Combined sources
Helixi75 – 828Combined sources
Helixi87 – 937Combined sources
Helixi95 – 1006Combined sources
Helixi105 – 1084Combined sources
Helixi109 – 1113Combined sources
Helixi116 – 1194Combined sources
Helixi122 – 13615Combined sources
Helixi140 – 1434Combined sources
Beta strandi144 – 1463Combined sources
Turni147 – 1493Combined sources
Helixi150 – 16415Combined sources
Helixi167 – 1704Combined sources
Turni171 – 1799Combined sources
Helixi180 – 1834Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 2037Combined sources
Helixi210 – 2167Combined sources
Helixi220 – 24930Combined sources
Beta strandi251 – 2533Combined sources
Helixi254 – 2574Combined sources
Helixi259 – 28628Combined sources
Helixi288 – 30619Combined sources
Helixi312 – 3187Combined sources
Helixi321 – 34020Combined sources
Helixi343 – 35412Combined sources
Turni355 – 3573Combined sources
Helixi358 – 3658Combined sources
Helixi367 – 3704Combined sources
Helixi372 – 3754Combined sources
Helixi377 – 39620Combined sources
Beta strandi408 – 4136Combined sources
Turni414 – 4163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the LacY/RafB permease family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
HOGENOMiHOG000114363.
InParanoidiP02920.
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

        10         20         30         40         50
MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA
60 70 80 90 100
AISLFSLLFQ PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ
110 120 130 140 150
YNILVGSIVG GIYLGFCFNA GAPAVEAFIE KVSRRSNFEF GRARMFGCVG
160 170 180 190 200
WALCASIVGI MFTINNQFVF WLGSGCALIL AVLLFFAKTD APSSATVANA
210 220 230 240 250
VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD QQFANFFTSF
260 270 280 290 300
FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS
310 320 330 340 350
VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY
360 370 380 390 400
LVCFCFFKQL AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL
410
SGPGPLSLLR RQVNEVA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P02920.
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: November 26, 2014
This is version 144 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