Protein Family Models

This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop. (from Pfam)

Date:

2024-08-14

This family contains ATPases involved in plasmid partitioning [1]. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits [2]. [1]. 2149583. A family of ATPases involved in active partitioning of diverse. bacterial plasmids.. Motallebi-Veshareh M, Rouch DA, Thomas CM;. Mol Microbiol 1990;4:1455-1463.. [2]. 15728363. The eukaryotic P loop NTPase Nbp35: an essential component of. the cytosolic and nuclear iron-sulfur protein assembly. machinery.. Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U,. Lill R;. Proc Natl Acad Sci U S A. 2005;102:3266-3271. (from Pfam)

Date:

2024-08-14

MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication [1]. It is responsible for the temporal and spatial regulation of FtsZ ring formation [1]. [1]. 16839883. MipZ, a spatial regulator coordinating chromosome segregation. with cell division in Caulobacter.. Thanbichler M, Shapiro L;. Cell. 2006;126:147-162. (from Pfam)

Date:

2024-08-14

This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed. [1]. 11260463. The multicellular morphotypes of Salmonella typhimurium and. Escherichia coli produce cellulose as the second component of. the extracellular matrix.. Zogaj X, Nimtz M, Rohde M, Bokranz W, Romling U;. Mol Microbiol 2001;39:1452-1463. (from Pfam)

Date:

2024-08-14

This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA Swiss:P29946 and CbiP Swiss:Q05597 from S.typhimurium [4], and CobQ Swiss:Q52686 from R. capsulatus [3]. These amidases catalyse amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria [4]. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family [6]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and. characterization of a Bacillus megaterium cobI operon.. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166.. [2]. 9742226. Cobalamin (vitamin B12) biosynthesis: functional. characterization of the Bacillus megaterium cbi genes required. to convert uroporphyrinogen III into cobyrinic acid a,c-diamide.. Raux E, Lanois A, Rambach A, Warren MJ, Thermes C;. Biochem J 1998;335:167-173.. [3]. 7635831. Identification and sequence analysis of genes involved in late. steps in cobalamin (vitamin B12) synthesis in Rhodobacter. capsulatus.. Pollich M, Klug G;. J Bacteriol 1995;177:4481-4487.. [4]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic. genes of Salmonella typhimurium.. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church. GM;. J Bacteriol 1993;175:3303-3316.. [5]. 10966576. The synthetase domains of cobalamin biosynthesis. amidotransferases cobB and cobQ belong to a . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell. [1]. 1704144. The plasmid-encoded arsenical resistance pump: an. anion-translocating ATPase.. Rosen BP;. Res Microbiol 1990;141:336-341. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14