8Y9Z
Structure of the SecA-SecY complex with the substrate HmBRI-3TM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006605 | biological_process | protein targeting |
A | 0008564 | molecular_function | protein-exporting ATPase activity |
A | 0015031 | biological_process | protein transport |
A | 0016020 | cellular_component | membrane |
A | 0031522 | cellular_component | cell envelope Sec protein transport complex |
A | 0043952 | biological_process | protein transport by the Sec complex |
A | 0045121 | cellular_component | membrane raft |
A | 0046872 | molecular_function | metal ion binding |
A | 0065002 | biological_process | intracellular protein transmembrane transport |
E | 0005886 | cellular_component | plasma membrane |
E | 0006605 | biological_process | protein targeting |
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 |
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 PROSITE/UniProt
site_id | PS00755 |
Number of Residues | 20 |
Details | SECY_1 Protein secY signature 1. SIFaMGVmPYItASIIVQLL |
Chain | Residue | Details |
Y | SER68-LEU87 |
site_id | PS00756 |
Number of Residues | 18 |
Details | SECY_2 Protein secY signature 2. WLgEqITak.GVGNGiSII |
Chain | Residue | Details |
Y | TRP165-ILE182 |
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYtDWlFTTPLLL |
Chain | Residue | Details |
B | ARG80-LEU92 |
site_id | PS01067 |
Number of Residues | 29 |
Details | SECE_SEC61G Protein secE/sec61-gamma signature. FfKEvVreLkKvsWPnrkElvnytAVVLA |
Chain | Residue | Details |
E | PHE7-ALA35 |
site_id | PS01312 |
Number of Residues | 16 |
Details | SECA SecA family signature. VtIATNMAGRGtDIkL |
Chain | Residue | Details |
A | VAL480-LEU495 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | GLU7-ALA27 | |
B | ILE42-PHE62 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Primary proton acceptor => ECO:0000250 |
Chain | Residue | Details |
B | ASP83 | |
A | GLY103 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM |
Chain | Residue | Details |
A | ASP492 |