MELY_ENTCC
ID MELY_ENTCC Reviewed; 425 AA.
AC P96517; A0A0H3CTM4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Melibiose permease {ECO:0000303|PubMed:18177889};
DE AltName: Full=Melibiose transporter MelY {ECO:0000305};
GN Name=melY {ECO:0000303|PubMed:9209070, ECO:0000303|PubMed:9375783};
GN OrderedLocusNames=ECL_05077 {ECO:0000312|EMBL:ADF64599.1};
OS Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=716541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC 279-56;
RX PubMed=9375783; DOI=10.1016/s0167-4781(97)00113-9;
RA Okazaki N., Jue X.X., Miyake H., Kuroda M., Shimamoto T., Tsuchiya T.;
RT "Sequence of a melibiose transporter gene of Enterobacter cloacae.";
RL Biochim. Biophys. Acta 1354:7-12(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC 279-56;
RX PubMed=9209070; DOI=10.1128/jb.179.13.4443-4445.1997;
RA Okazaki N., Jue X.X., Miyake H., Kuroda M., Shimamoto T., Tsuchiya T.;
RT "A melibiose transporter and an operon containing its gene in Enterobacter
RT cloacae.";
RL J. Bacteriol. 179:4443-4445(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC 279-56;
RX PubMed=20207761; DOI=10.1128/jb.00067-10;
RA Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT strain ATCC 13047.";
RL J. Bacteriol. 192:2463-2464(2010).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-88; LEU-91
RP AND ALA-182.
RX PubMed=12775706; DOI=10.1128/jb.185.12.3672-3677.2003;
RA Shinnick S.G., Perez S.A., Varela M.F.;
RT "Altered substrate selection of the melibiose transporter (MelY) of
RT Enterobacter cloacae involving point mutations in Leu-88, Leu-91, and Ala-
RT 182 that confer enhanced maltose transport.";
RL J. Bacteriol. 185:3672-3677(2003).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ALA-367.
RX PubMed=18177889; DOI=10.1016/j.jmb.2007.12.015;
RA Tavoulari S., Frillingos S.;
RT "Substrate selectivity of the melibiose permease (MelY) from Enterobacter
RT cloacae.";
RL J. Mol. Biol. 376:681-693(2008).
CC -!- FUNCTION: Responsible for transport of melibiose into the cell, with
CC the concomitant import of a proton (symport system) (PubMed:9209070,
CC PubMed:9375783, PubMed:12775706, PubMed:18177889). Can also transport
CC lactose, and has weak activity with maltose (PubMed:18177889,
CC PubMed:12775706). Cannot transport the analog methyl-1-thio-beta,D-
CC galactopyranoside (TMG) (PubMed:18177889).
CC {ECO:0000269|PubMed:12775706, ECO:0000269|PubMed:18177889,
CC ECO:0000269|PubMed:9209070, ECO:0000269|PubMed:9375783}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for melibiose {ECO:0000269|PubMed:18177889};
CC KM=0.51 mM for lactose {ECO:0000269|PubMed:18177889};
CC KM=14 mM for maltose {ECO:0000269|PubMed:12775706};
CC Vmax=82 nmol/min/mg enzyme with melibiose as substrate
CC {ECO:0000269|PubMed:18177889};
CC Vmax=54 nmol/min/mg enzyme with lactose as substrate
CC {ECO:0000269|PubMed:18177889};
CC Vmax=121 nmol/min/mg enzyme with maltose as substrate
CC {ECO:0000269|PubMed:12775706};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Oligosaccharide:H(+) symporter (OHS) (TC 2.A.1.5) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB000622; BAA19154.1; -; Genomic_DNA.
DR EMBL; CP001918; ADF64599.1; -; Genomic_DNA.
DR RefSeq; WP_013099342.1; NC_014121.1.
DR RefSeq; YP_003615548.1; NC_014121.1.
DR AlphaFoldDB; P96517; -.
DR SMR; P96517; -.
DR STRING; 716541.ECL_05077; -.
DR TCDB; 2.A.1.5.4; the major facilitator superfamily (mfs).
DR EnsemblBacteria; ADF64599; ADF64599; ECL_05077.
DR KEGG; enc:ECL_05077; -.
DR PATRIC; fig|716541.4.peg.5208; -.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_055585_0_0_6; -.
DR OMA; FIMATCF; -.
DR Proteomes; UP000002363; 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:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR000576; LacY/RafB_perm_fam.
DR InterPro; IPR018457; LacY/RafB_perm_fam_CS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF01306; LacY_symp; 1.
DR PRINTS; PR00174; LACYSMPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00882; 2A0105; 1.
DR PROSITE; PS00896; LACY_1; 1.
DR PROSITE; PS00897; LACY_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..425
FT /note="Melibiose permease"
FT /id="PRO_0000442742"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..50
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..107
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..267
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..325
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..385
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12775706"
FT MUTAGEN 88
FT /note="L->P: Does not affect melibiose transport. Increases
FT affinity for maltose and maltose transport."
FT /evidence="ECO:0000269|PubMed:12775706"
FT MUTAGEN 91
FT /note="L->P: Does not affect melibiose transport. Increases
FT affinity for maltose and maltose transport."
FT /evidence="ECO:0000269|PubMed:12775706"
FT MUTAGEN 182
FT /note="A->P: Does not affect melibiose transport. Increases
FT affinity for maltose and maltose transport."
FT /evidence="ECO:0000269|PubMed:12775706"
FT MUTAGEN 367
FT /note="A->V: No change in transport activity."
FT /evidence="ECO:0000269|PubMed:18177889"
SQ SEQUENCE 425 AA; 46701 MW; D49AF033F9105D51 CRC64;
MNTTTCTHKD NPNFWIFGLF FFLYFFIMAT CFPFLPIWLS DIIGLNKTHT GIVFSCISLS
AIAFQPVLGV ISDKLGLKKH LLWIISVLLF LFAPFFLYVF APLLKTNIWL GALSGGLYIG
FVFSAGSGAI EAYIERVSRN SAFEYGKARM FGCLGWGLCA STGGILFGID PSYVFWMGSA
AALLLMLLLV VAKPKPNQTA QVMNALGANQ PQITAKKVFN LFRQRRMWMF ILYVIGVACV
YDVFDQQFAT FFKTFFATPQ EGTRAFGFAT TAGEICNAII MFCSPWIINR IGAKNTLLIA
GLIMATRIIG SSFATTAVEV IALKMLHALE VPFLLVGAFK YITGVFDTRL SATIYLIGFQ
FAKQSAAIFL SAFAGNMYDR IGFQETYLML GCFVLAITVV SAFTLSSRQE IAAAAGAAAL
TSQSR
