LACY_LACDA
ID LACY_LACDA Reviewed; 627 AA.
AC P22733; Q1G9Z3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Lactose permease;
DE AltName: Full=Lactose transport protein;
DE AltName: Full=Lactose-proton symporter;
DE Includes:
DE RecName: Full=Putative phosphotransferase enzyme IIA component;
DE EC=2.7.1.-;
DE AltName: Full=Putative PTS system EIIA component;
GN Name=lacY; OrderedLocusNames=Ldb1202;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1705929; DOI=10.1128/jb.173.6.1951-1957.1991;
RA Leong-Morgenthaler P.M., Zwahlen M.-C., Hottinger H.;
RT "Lactose metabolism in Lactobacillus bulgaricus: analysis of the primary
RT structure and expression of the genes involved.";
RL J. Bacteriol. 173:1951-1957(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- FUNCTION: Responsible for transport of beta-galactosides into the cell,
CC with the concomitant uptake of protons (symport system), and also for
CC transport of homologous and heterologous exchange of beta-galactosides.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The PTS EIIA type-1 domain may serve a regulatory function,
CC through its phosphorylation activity.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC sodium:galactoside symporter (TC 2.A.2) family. {ECO:0000305}.
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DR EMBL; M55068; AAA25243.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI98004.1; -; Genomic_DNA.
DR PIR; A38538; A38538.
DR RefSeq; WP_011543943.1; NZ_JQAV01000039.1.
DR AlphaFoldDB; P22733; -.
DR SMR; P22733; -.
DR STRING; 390333.Ldb1202; -.
DR EnsemblBacteria; CAI98004; CAI98004; Ldb1202.
DR KEGG; ldb:Ldb1202; -.
DR PATRIC; fig|390333.13.peg.1438; -.
DR eggNOG; COG2190; Bacteria.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_027408_1_0_9; -.
DR OMA; DIPYWSM; -.
DR BioCyc; LDEL390333:LDB_RS05150-MON; -.
DR Proteomes; UP000001259; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR001927; Na/Gal_symport.
DR InterPro; IPR018043; Na/Gal_symport_CS.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR PANTHER; PTHR11328; PTHR11328; 1.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR TIGRFAMs; TIGR00792; gph; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR PROSITE; PS00872; NA_GALACTOSIDE_SYMP; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Symport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..627
FT /note="Lactose permease"
FT /id="PRO_0000170757"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 493..597
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT REGION 1..460
FT /note="Permease"
FT MOD_RES 545
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 68289 MW; 809367A40DD34050 CRC64;
MKKKLVSRLS YAAGAFGNDV FYATLSTYFI VFVTTHLFNA GDHKMIFIIT NLITAIRIGE
VLLDPLIGNA IDRTESRWGK FKPWVVGGGI ISSLALLALF TDFGGINQSK PVVYLVIFGI
VYLIMDIFYS FKDTGFWAMI PALSLDSRER EKTSTFARVG STIGANLVGV VITPIILFFS
ASKANPNGDK QGWFFFALIV AIVGILTSIT VGLGTHEVKS ALRESNEKTT LKQVFKVLGQ
NDQLLWLAFA YWFYGLGINT LNALQLYYFS YILGDARGYS LLYTINTFVG LISASFFPSL
AKKFNRNRLF YACIAVMLLG IGVFSVASGS LALSLVGAEF FFIPQPLAFL VVLMIISDAV
EYGQLKTGHR DEALTLSVRP LVDKLGGALS NWFVSLIALT AGMTTGATAS TITAHGQMVF
KLAMFALPAV MLLIAVSIFA KKVFLTEEKH AEIVDQLETQ FGQSHAQKPA QAESFTLASP
VSGQLMNLDM VDDPVFADKK LGDGFALVPA DGKVYAPFAG TVRQLAKTRH SIVLENEHGV
LVLIHLGLGT AKLNGTGFVS YVEEGSQVEA GQQILEFWDP AIKQAKLDDT VIVTVINSET
FANSQMLLPI GHSVQALDDV FKLEGKN
