Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006605 | biological_process | protein targeting |
| E | 0006886 | biological_process | intracellular protein transport |
| E | 0008320 | molecular_function | protein transmembrane transporter activity |
| E | 0009306 | biological_process | protein secretion |
| E | 0015031 | biological_process | protein transport |
| E | 0016020 | cellular_component | membrane |
| E | 0043952 | biological_process | protein transport by the Sec complex |
| E | 0065002 | biological_process | intracellular protein transmembrane transport |
| G | 0009306 | biological_process | protein secretion |
| G | 0015450 | molecular_function | protein-transporting ATPase activity |
| G | 0016020 | cellular_component | membrane |
| Y | 0005886 | cellular_component | plasma membrane |
| Y | 0006605 | biological_process | protein targeting |
| Y | 0015031 | biological_process | protein transport |
| Y | 0016020 | cellular_component | membrane |
| Y | 0043952 | biological_process | protein transport by the Sec complex |
| Y | 0065002 | biological_process | intracellular protein transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue OLC Y 501 |
| Chain | Residue |
| G | ASP2 |
| Y | ASN294 |
| Y | LEU297 |
| Y | OLC506 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue OLC Y 502 |
| Chain | Residue |
| Y | OLC503 |
| Y | OLC506 |
| Y | PRO151 |
| Y | PHE291 |
| Y | ASP293 |
| Y | ASN294 |
| Y | LEU297 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue OLC Y 503 |
| Chain | Residue |
| Y | THR132 |
| Y | OLC502 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue OLC Y 504 |
| Chain | Residue |
| E | TRP21 |
| G | MET1 |
| Y | TRP370 |
| Y | PHE374 |
| Y | LEU377 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLC Y 505 |
| Chain | Residue |
| G | OLC103 |
| Y | OLC507 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue OLC Y 506 |
| Chain | Residue |
| G | TYR5 |
| G | TRP73 |
| G | PRO74 |
| G | OLC101 |
| Y | GLY146 |
| Y | SER148 |
| Y | PHE152 |
| Y | PHE155 |
| Y | OLC501 |
| Y | OLC502 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue OLC Y 507 |
| Chain | Residue |
| G | OLC103 |
| Y | PRO309 |
| Y | SER310 |
| Y | LEU312 |
| Y | PHE313 |
| Y | LEU380 |
| Y | ILE384 |
| Y | OLC505 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC G 101 |
| Chain | Residue |
| G | TYR5 |
| G | LEU10 |
| G | LEU13 |
| Y | OLC506 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue OLC G 102 |
| Chain | Residue |
| G | TYR53 |
| Y | LEU23 |
| Y | ALA27 |
| Y | ILE34 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue OLC G 103 |
| Chain | Residue |
| G | ARG54 |
| G | VAL62 |
| Y | ASN387 |
| Y | OLC505 |
| Y | OLC507 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 27 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mvkafwsalqipelrqrvl................................................................................................FTLLVLAA |
| Chain | Residue | Details |
| Y | MET1-ALA27 | |
| site_id | PS00756 |
| Number of Residues | 18 |
| Details | SECY_2 Protein secY signature 2. WMaErITey.GIGNGtSLI |
| Chain | Residue | Details |
| Y | TRP170-ILE187 | |
| site_id | PS01067 |
| Number of Residues | 29 |
| Details | SECE_SEC61G Protein secE/sec61-gamma signature. YfQEaRaeLaRvtWPtreQvvegtQAILL |
| Chain | Residue | Details |
| E | TYR8-LEU36 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 166 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 75 |
| Details | Topological domain: {"description":"Periplasmic"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Discontinuously helical; Name=2"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Intramembrane: {"description":"Helical; Name=Helix 2A"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Intramembrane: {} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 15 |
| Details | Intramembrane: {"description":"Helical; Name=Helix 2B"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 15 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=8"} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=9"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 15 |
| Details | Transmembrane: {"description":"Helical; Name=10"} |
| site_id | SWS_FT_FI16 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical"} |
| site_id | SWS_FT_FI17 |
| Number of Residues | 7 |
| Details | Topological domain: {"description":"Extracellular"} |