RAFB_ECOLX
ID RAFB_ECOLX Reviewed; 425 AA.
AC P16552;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Raffinose permease {ECO:0000303|PubMed:18008022};
DE Short=Raf permease {ECO:0000303|PubMed:2556373};
GN Name=rafB {ECO:0000303|PubMed:2556373};
OS Escherichia coli.
OG Plasmid pRSD2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=2556373; DOI=10.1128/jb.171.12.6753-6763.1989;
RA Aslanidis C., Schmid K., Schmitt R.;
RT "Nucleotide sequences and operon structure of plasmid-borne genes mediating
RT uptake and utilization of raffinose in Escherichia coli.";
RL J. Bacteriol. 171:6753-6763(1989).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF VAL-35; SER-138; SER-139; GLY-389 AND ILE-391.
RX PubMed=18008022; DOI=10.1007/s00232-007-9077-1;
RA Van Camp B.M., Crow R.R., Peng Y., Varela M.F.;
RT "Amino acids that confer transport of raffinose and maltose sugars in the
RT raffinose permease (RafB) of Escherichia coli as implicated by spontaneous
RT mutations at Val-35, Ser-138, Ser-139, Gly-389 and Ile-391.";
RL J. Membr. Biol. 220:87-95(2007).
CC -!- FUNCTION: Responsible for transport of raffinose into the cell
CC (PubMed:2556373, PubMed:18008022). Can also transport lactose and
CC melibiose (PubMed:2556373). Has weak activity with maltose
CC (PubMed:18008022). {ECO:0000269|PubMed:18008022,
CC ECO:0000269|PubMed:2556373}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for raffinose {ECO:0000269|PubMed:2556373};
CC KM=0.6 mM for lactose {ECO:0000269|PubMed:2556373};
CC KM=0.06 mM for melibiose {ECO:0000269|PubMed:2556373};
CC Vmax=360 nmol/min/mg enzyme with raffinose as substrate
CC {ECO:0000269|PubMed:2556373};
CC Vmax=100 nmol/min/mg enzyme with lactose as substrate
CC {ECO:0000269|PubMed:2556373};
CC Vmax=37 nmol/min/mg enzyme with melibiose as substrate
CC {ECO:0000269|PubMed:2556373};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P02920}.
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}.
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DR EMBL; M27273; AAA24498.1; -; Genomic_DNA.
DR PIR; B43717; B43717.
DR AlphaFoldDB; P16552; -.
DR SMR; P16552; -.
DR TCDB; 2.A.1.5.2; the major facilitator superfamily (mfs).
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; Plasmid; Sugar transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..425
FT /note="Raffinose permease"
FT /id="PRO_0000196187"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..48
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..105
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..265
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..383
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18008022"
FT SITE 129
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT SITE 147
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT SITE 272
FT /note="Substrate binding and proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT SITE 305
FT /note="Proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT SITE 325
FT /note="Proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT SITE 328
FT /note="Proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P02920"
FT MUTAGEN 35
FT /note="V->A: Significantly reduces raffinose transport,
FT enhances maltose transport."
FT /evidence="ECO:0000269|PubMed:18008022"
FT MUTAGEN 138
FT /note="S->D: Significantly reduces raffinose transport,
FT enhances maltose transport; when associated with L-139 and
FT A-389."
FT /evidence="ECO:0000269|PubMed:18008022"
FT MUTAGEN 139
FT /note="S->L: Significantly reduces raffinose transport,
FT enhances maltose transport; when associated with D-138 and
FT A-389."
FT /evidence="ECO:0000269|PubMed:18008022"
FT MUTAGEN 389
FT /note="G->A: Significantly reduces raffinose transport,
FT enhances maltose transport; when associated with D-138 and
FT L-139."
FT /evidence="ECO:0000269|PubMed:18008022"
FT MUTAGEN 391
FT /note="I->S: Significantly reduces raffinose transport,
FT enhances maltose transport."
FT /evidence="ECO:0000269|PubMed:18008022"
SQ SEQUENCE 425 AA; 46693 MW; CAEA12A78B8B1A1C CRC64;
MNSASTHKNT DFWIFGLFFF LYFFIMATCF PFLPVWLSDV VGLSKTDTGI VFSCLSLFAI
SFQPLLGVIS DRLGLKKNLI WSISLLLVFF APFFLYVFAP LLHLNIWAGA LTGGVFIGFV
FSAGAGAIEA YIERVSRSSG FEYGKARMFG CLGWALCATM AGILFNVDPS LVFWMGSGGA
LLLLLLLYLA RPSTSQTAMV MNALGANSSL ISTRMVFSLF RMRQMWMFVL YTIGVACVYD
VFDQQFAIFF RSFFDTPQAG IKAFGFATTA GEICNAIIMF CTPWIINRIG AKNTLLVAGG
IMTIRITGSA FATTMTEVVI LKMLHALEVP FLLVGAFKYI TGVFDTRLSA TVYLIGFQFS
KQLAAILLST FAGHLYDRMG FQNTYFVLGM IVLTVTVISA FTLSSSPGIV HPSVEKAPVA
HSEIN
