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Links from Protein

Items: 11

1.

cysteine peptidase family C39 domain-containing protein

This domain often occurs confers as the leader peptidase domain of transporter subunits involved in cleaving peptides or proteins, such as bacteriocins with a double-glycine type leader peptide, during export.

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
peptidase activity (GO:0008233)
Cellular Component:
membrane (GO:0016020)
Date:
2024-10-16
Family Accession:
NF015377.5
Method:
HMM
2.

ABC transporter transmembrane domain-containing protein

This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (Pfam:PF00005) have two such regions. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
membrane (GO:0016020)
Molecular Function:
ATPase-coupled transmembrane transporter activity (GO:0042626)
Biological Process:
transmembrane transport (GO:0055085)
Molecular Function:
ABC-type transporter activity (GO:0140359)
Date:
2024-08-14
Family Accession:
NF012869.5
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
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.

NHLP family bacteriocin export ABC transporter peptidase/permease/ATPase subunit

This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin.

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
peptidase activity (GO:0008233)
Biological Process:
transmembrane transport (GO:0055085)
Molecular Function:
ABC-type transporter activity (GO:0140359)
Date:
2021-10-15
Family Accession:
TIGR03796.1
Method:
HMM
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