8PB9
Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051782 | biological_process | negative regulation of cell division |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0051782 | biological_process | negative regulation of cell division |
C | 0005524 | molecular_function | ATP binding |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0008134 | molecular_function | transcription factor binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0008134 | molecular_function | transcription factor binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0008134 | molecular_function | transcription factor binding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PROSITE/UniProt
site_id | PS00675 |
Number of Residues | 14 |
Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIlGESGTGKevV |
Chain | Residue | Details |
D | VAL170-VAL183 |
site_id | PS00676 |
Number of Residues | 16 |
Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFelANGGTLFLDEI |
Chain | Residue | Details |
D | GLY232-ILE247 |
site_id | PS00688 |
Number of Residues | 10 |
Details | SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNVRELaN |
Chain | Residue | Details |
D | TRP358-ASN367 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:28065505, ECO:0007744|PDB:5J1J |
Chain | Residue | Details |
A | LYS19 | |
B | ARG221 | |
A | GLU153 | |
A | ASN181 | |
A | PRO215 | |
A | ARG221 | |
B | LYS19 | |
B | GLU153 | |
B | ASN181 | |
B | PRO215 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26712005, ECO:0007744|PDB:5EXT |
Chain | Residue | Details |
D | VAL147 | |
E | GLY177 | |
E | ARG334 | |
E | ARG363 | |
D | GLY177 | |
D | ARG334 | |
D | ARG363 | |
C | VAL147 | |
C | GLY177 | |
C | ARG334 | |
C | ARG363 | |
E | VAL147 |