Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008963 | molecular_function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
A | 0042802 | molecular_function | identical protein binding |
A | 0044038 | biological_process | cell wall macromolecule biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051301 | biological_process | cell division |
A | 0051992 | molecular_function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity |
A | 0071555 | biological_process | cell wall organization |
B | 0005886 | cellular_component | plasma membrane |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008963 | molecular_function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016740 | molecular_function | transferase activity |
B | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
B | 0042802 | molecular_function | identical protein binding |
B | 0044038 | biological_process | cell wall macromolecule biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051301 | biological_process | cell division |
B | 0051992 | molecular_function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 136 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | MET1-ARG25 | |
A | HIS219-TYR233 | |
A | LEU281-SER284 | |
A | LEU356-ARG359 | |
B | MET93-LYS98 | |
B | ASP153-VAL172 | |
B | HIS219-TYR233 | |
B | LEU281-SER284 | |
B | LEU356-ARG359 | |
A | MET1-ARG25 | |
A | MET93-LYS98 | |
A | ASP153-VAL172 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=Helix 1 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | SER26-LEU48 | |
A | SER26-LEU48 |
site_id | SWS_FT_FI3 |
Number of Residues | 130 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | ARG49-PRO74 | |
A | TRP311-LEU332 | |
B | LYS121-ILE130 | |
B | LEU195-GLY197 | |
B | SER256-GLY264 | |
B | TRP311-LEU332 | |
A | ARG49-PRO74 | |
A | LYS121-ILE130 | |
A | LEU195-GLY197 | |
A | SER256-GLY264 |
site_id | SWS_FT_FI4 |
Number of Residues | 34 |
Details | TRANSMEM: Helical; Name=Helix 2 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | THR75-LEU92 | |
A | THR75-LEU92 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Helix 3 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | TYR99-VAL120 | |
A | TYR99-VAL120 |
site_id | SWS_FT_FI6 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Helix 4 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | LYS131-ALA152 | |
A | LYS131-ALA152 |
site_id | SWS_FT_FI7 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Helix 5 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | LEU173-GLY194 | |
A | LEU173-GLY194 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=Helix 6 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | LEU198-GLY218 | |
A | LEU198-GLY218 |
site_id | SWS_FT_FI9 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Helix 7 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | ALA234-ASN255 | |
A | ALA234-ASN255 |
site_id | SWS_FT_FI10 |
Number of Residues | 30 |
Details | TRANSMEM: Helical; Name=Helix 8 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | ASP265-LEU280 | |
A | ASP265-LEU280 |
site_id | SWS_FT_FI11 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=Helix 9 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | GLU285-ARG310 | |
A | GLU285-ARG310 |
site_id | SWS_FT_FI12 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=Helix 10 => ECO:0000269|PubMed:23990562 |
Chain | Residue | Details |
B | PRO333-MET355 | |
A | PRO333-MET355 |
site_id | SWS_FT_FI13 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR |
Chain | Residue | Details |
B | LYS70 | |
A | LYS70 | |
A | THR75 | |
A | ASN190 | |
A | ASP193 | |
A | ASP196 | |
A | GLY264 | |
A | SER268 | |
A | GLN305 | |
A | ALA321 | |
B | THR75 | |
B | ASN190 | |
B | ASP193 | |
B | ASP196 | |
B | GLY264 | |
B | SER268 | |
B | GLN305 | |
B | ALA321 |