Protein Family Models

This entry is the BID (Bep intracellular delivery) domain located at the C-terminal of Bartonella effector proteins (Beps). It functions as a secretion signal in a subfamily of protein substrates of bacterial type IV secretion (T4S) systems. It mediates transfer of (1) relaxases and the attached DNA during bacterial conjugation, and (2) numerous Beps during protein transfer into host cells infected by pathogenic Bartonella species. Crystal structure of several representative BID domains show a conserved fold characterized by a compact, antiparallel four-helix bundle topped with a hook [1]. [1]. 27889208. The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook. Stanger FV, de Beer TA, Dranow DM, Schirmer T, Phan I, Dehio C;. Structure. 2017;25:203-211. (from Pfam)

Date:

2024-10-16

This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

This family includes of the MobA protein from the E. coli plasmid RSF1010, and the MobL protein from the Thiobacillus ferrooxidans plasmid PTF1. These sequences are mobilisation proteins, which are essential for specific plasmid transfer. (from Pfam)

Date:

2024-08-14

Helicase activity for this family has been demonstrated [1] and NTPase activity [2]. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis [3]. This family is discussed pages 388-391. [1]. 8269709. Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Koonin EV, Dolja VV;. Crit Rev Biochem Mol Biol 1993;28:375-430. [2]. 10217401. RNA helicase activity of Semliki Forest virus replicase protein NSP2. Gomez de Cedron M, Ehsani N, Mikkola ML, Garcia JA, Kaariainen L;. FEBS Lett 1999;448:19-22. [3]. 8057461. ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. Rikkonen M, Peranen J, Kaariainen L;. J Virol 1994;68:5804-5810. [4]. 10982322. Helicase and capping enzyme active site mutations in brome mosaic virus protein 1a cause defects in template recruitment, negative-strand RNA synthesis, and viral RNA capping. Ahola T, den Boon JA, Ahlquist P;. J Virol 2000;74:8803-8811. (from Pfam)

Date:

2024-10-16

PRK13826 family protein

Date:

2017-03-02

This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, PF03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer [1].

Gene:

traA

Date:

2021-08-31

Date:

2020-10-26