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Links from Protein

Items: 8

1.

TerB family tellurite resistance protein

This family contains the TerB tellurite resistance proteins from a a number of bacteria. [1]. 3049247. The nucleotide sequence of a plasmid determinant for resistance to tellurium anions. Jobling MG, Ritchie DA;. Gene 1988;66:245-258. [2]. 10069007. In vivo and in vitro cloning and phenotype characterization of tellurite resistance determinant conferred by plasmid pTE53 of a clinical isolate of Escherichia coli. Burian J, Tu N, Kl'ucar L, Guller L, Lloyd-Jones G, Stuchlik S, Fejdi P, Siekel P, Turna J;. Folia Microbiol (Praha) 1998;43:589-599. (from Pfam)

Date:
2024-10-16
Family Accession:
NF016955.5
Method:
HMM
2.

DnaJ domain-containing protein

DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature [2]. [1]. 8016869. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Cyr DM, Langer T, Douglas MG;. Trends Biochem Sci 1994;19:176-181. [2]. 9271376. Inactivation of pRB-related proteins p130 and p107 mediated by the J domain of simian virus 40 large T antigen. Stubdal H, Zalvide J, Campbell KS, Schweitzer C, Roberts TM, DeCaprio JA;. Mol Cell Biol 1997;17:4979-4990. The structure of the DnaJ domain by NMR. [3]. 8764403. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wuthrich K;. J Mol Biol 1996;260:236-250. [4]. 9644977. The J-domain family and the recruitment of chaperone power. Kelley WL;. Trends Biochem Sci 1998;23:222-227. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012451.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
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.

co-chaperone DjlA

co-chaperone DjlA (DnaJ-like protein A) is an inner membrane-associated bacterial co-chaperone for DnaK

Date:
2021-02-03
Family Accession:
11484161
Method:
Sparcle
8.

co-chaperone DjlA

Functions as a co-chaperone with DnaK; involved in regulation of colanic acid capsule; J-like domain is cytoplasmic and can Functionally substitute for DnaJ; stimulates synthesis of colanic acid mucoid capsule through the RcsB/C signal transduction system

Gene:
djlA
GO Terms:
Molecular Function:
protein-folding chaperone binding (GO:0051087)
Date:
2021-08-26
Family Accession:
NF006948.0
Method:
HMM
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