GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:10358096
A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase.
PMID:15690043
Interaction network containing conserved and essential protein complexes in Escherichia coli.
PMID:158358
Properties of membranes from mutant strains of Escherichia coli in which the beta-subunit of the adenosine triphosphatase is abnormal.
PMID:16079137
Protein complexes of the Escherichia coli cell envelope.
PMID:16606699
Large-scale identification of protein-protein interaction of Escherichia coli K-12.
PMID:16858726
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
PMID:17137328
Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins.
PMID:21602818
Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.
PMID:24561554
The binary protein-protein interaction landscape of Escherichia coli.
PMID:28001127
Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states.
PMID:2863270
Assembly of a functional F1 of the proton-translocating ATPase of Escherichia coli.
PMID:2874137
Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli.
file:ECOLI/atpD/atpD-uniprot.txt
UniProtKB P0ABB4 (ATPB_ECOLI) entry
PMID:1832155
Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase.
PMID:2859284
The defective proton-ATPase of uncD mutants of Escherichia coli. Two mutations which affect the catalytic mechanism.
PMID:7479919
Rotation of subunits during catalysis by Escherichia coli F1-ATPase.