Protein Family Models

Zincin-like Metallopeptidase frequently found in polyvalent proteins of phages and conjugative elements. The active site is comprised of a HEXXH motif and a C-terminal glutamate [1]. [1]. 28559295. Polyvalent Proteins, a Pervasive Theme in the Intergenomic. Biological Conflicts of Bacteriophages and Conjugative Elements.. Iyer LM, Burroughs AM, Anand S, de Souza RF, Aravind L;. J Bacteriol. 2017; [Epub ahead of print] (from Pfam)

Date:

2024-08-14

This is the ssDNA binding domain of anti-restriction factor ArdC deployed by plasmids and phages in polyvalent proteins related to the BHD domains of XPC/Rad4 and the Tc-38 domain found in kinetoplastid minicircle binding proteins [1,2,3]. The structure of this domain is composed of three alpha-helices and a three-stranded beta-sheet that supports a long and protuberant beta-hairpin [3]. This domain is also found in the N-terminal region of the RP4 TraC1 primase [4], together with the Toprim domain (pfam:PF01751, pfam:PF13362 and pfam:PF13662). [1]. 30396152. Unexpected Evolution of Lesion-Recognition Modules in Eukaryotic. NER and Kinetoplast DNA Dynamics Proteins from Bacterial Mobile. Elements.. Krishnan A, Burroughs AM, Iyer LM, Aravind L;. iScience. 2018;9:192-208.. [2]. 28559295. Polyvalent Proteins, a Pervasive Theme in the Intergenomic. Biological Conflicts of Bacteriophages and Conjugative Elements.. Iyer LM, Burroughs AM, Anand S, de Souza RF, Aravind L;. J Bacteriol. 2017; [Epub ahead of print]. [3]. 32348296. ArdC, a ssDNA-binding protein with a metalloprotease domain,. overpasses the recipient hsdRMS restriction system broadening. conjugation host range.. Gonzalez-Montes L, Del Campo I, Garcillan-Barcia MP, de la Cruz. F, Moncalian G;. PLoS Genet. 2020;16:e1008750.. [4]. 10686096. Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa. has a high similarity to the "protein transport" domain of TraC1. primase of promiscuous plasmid RP4.. Belogurov AA, Delver EP, Agafonova OV, Belogurova NG, Lee LY,. Kado CI;. J Mol Biol. 2000;296:969-977. (from Pfam)

Date:

2024-08-14

This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR [2]. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae [1], HTH-type transcriptional regulators RamB [3] and PrpC [4]. [1]. 19150362. Crystal structure of the IrrE protein, a central regulator of. DNA damage repair in deinococcaceae.. Vujicic-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P,. Sommer S, de Groot A, Serre L;. J Mol Biol. 2009;386:704-716.. [2]. 18761623. A conserved anti-repressor controls horizontal gene transfer by. proteolysis.. Bose B, Auchtung JM, Lee CA, Grossman AD;. Mol Microbiol. 2008;70:570-582.. [3]. 15090522. RamB, a novel transcriptional regulator of genes involved in. ac. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14