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Links from Protein

Items: 11

1.

AAA family ATPase

Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
ATP hydrolysis activity (GO:0016887)
Date:
2024-08-14
Family Accession:
NF024700.5
Method:
HMM
2.

Oligopeptide/dipeptide transporter, C-terminal region

This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (Pfam:PF00005). All characterised members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. (from Pfam)

GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
peptide transport (GO:0015833)
Date:
2024-08-14
Family Accession:
NF019951.5
Method:
HMM
3.

ATP-binding cassette domain-containing protein

ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains. [1]. 1864505. Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Rosteck PR Jr, Reynolds PA, Hershberger CL;. Gene 1991;102:27-32. [2]. 1977073. Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB;. Mol Microbiol 1990;4:873-880. [3]. 2229036. Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP;. J Bioenerg Biomembr 1990;22:571-592. [4]. 9872322. Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH;. Nature 1998;396:703-707. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Date:
2024-10-16
Family Accession:
NF012235.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

oligopeptide/dipeptide ABC transporter ATP-binding protein

This HMM represents a domain found in the C-terminal regions of ABC transporter ATP binding proteins, immediately following the ATP-binding domain (PF00005). Many are involved in the transport of oligopeptides or dipeptides, including E. coli K-12 proteins DppD (dipeptide/heme), OppD and OppF (oligopeptide), DdpD and DdpF (D,D-dipeptide), etc.

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasmic side of plasma membrane (GO:0009898)
Molecular Function:
ABC-type peptide transporter activity (GO:0015440)
Biological Process:
peptide transport (GO:0015833)
Cellular Component:
ATP-binding cassette (ABC) transporter complex (GO:0043190)
Date:
2023-11-07
Family Accession:
TIGR01727.1
Method:
HMM
11.

ABC transporter ATP-binding protein

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including dipeptides and oligopeptides

Date:
2024-04-15
Family Accession:
11418519
Method:
Sparcle
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