Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005351 | molecular_function | carbohydrate:proton symporter activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008643 | biological_process | carbohydrate transport |
| A | 0015293 | molecular_function | symporter activity |
| A | 0015528 | molecular_function | lactose:proton symporter activity |
| A | 0015767 | biological_process | lactose transport |
| A | 0016020 | cellular_component | membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0030395 | molecular_function | lactose binding |
| A | 0034219 | biological_process | carbohydrate transmembrane transport |
| A | 0055085 | biological_process | transmembrane transport |
| A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG A 501 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 502 |
| Chain | Residue |
| A | PHE21 |
| A | ILE22 |
| A | LEU172 |
| A | CYS176 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 503 |
| Chain | Residue |
| A | LEU57 |
| A | CYS355 |
| A | PHE356 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 505 |
| Chain | Residue |
| A | GLY231 |
| A | CYS234 |
| A | THR235 |
| A | MET365 |
| A | ILE230 |
Functional Information from PROSITE/UniProt
| site_id | PS00896 |
| Number of Residues | 15 |
| Details | LACY_1 LacY family proton/sugar symporters signature 1. GLLsDKLGLRKyLLW |
| Chain | Residue | Details |
| A | GLY64-TRP78 | |
| site_id | PS00897 |
| Number of Residues | 15 |
| Details | LACY_2 LacY family proton/sugar symporters signature 2. PlIINRIGgKNALLL |
| Chain | Residue | Details |
| A | PRO280-LEU294 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2164211","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2164211","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=8"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=9"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=10"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=11"} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=12"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2164211","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Site: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"12893935","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Site: {"description":"Substrate binding and proton translocation","evidences":[{"source":"PubMed","id":"12893935","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI18 |
| Number of Residues | 3 |
| Details | Site: {"description":"Proton translocation","evidences":[{"source":"PubMed","id":"12893935","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-formylmethionine; partial","evidences":[{"source":"PubMed","id":"10485888","evidenceCode":"ECO:0000269"}]} |
