Protein Family Models

Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides [2]. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan [1]. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats [1]. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localises to the septum ring complex. [1]. 16042392. Solution Structure of the Peptidoglycan Binding Domain of Bacillus subtilis Cell Wall Lytic Enzyme CwlC: Characterization of the Sporulation-Related Repeats by NMR(,). Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C;. Biochemistry 2005;44:10153-10163. [2]. 26305949. Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides. Yahashiri A, Jorgenson MA, Weiss DS;. Proc Natl Acad Sci U S A. 2015;112:11347-11352. (from Pfam)

Date:

2024-10-16

Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold [3,4]. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli [1]. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity [5]. [1]. 8576052. Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. Bass S, Gu Q, Christen A;. J Bacteriol 1996;178:1154-1161. [2]. 3316191. Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome. Takase I, Ishino F, Wachi M, Kamata H, Doi M, Asoh S, Matsuzawa H, Ohta T, Matsuhashi M;. J Bacteriol 1987;169:5692-5699. [3]. 10610264. N-ethylmaleimide-sensitive fusion protein (NSF) and CDC48 confirmed as members of the double-psi beta-barrel aspartate decarboxylase/formate dehydrogenase family. Mizuguchi K, Dhanaraj V, Blundell TL, Murzin AG;. Structure Fold Des. 1999;7:215-216. [4]. 10368289. A six-stranded double-psi beta barrel is shared by several protein superfamilies. Castillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG;. Structure Fold Des 1999;7:227-236. [5]. . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

septal ring lytic transglycosylase RlpA family protein similar to endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides

Date:

2018-08-09

Gene:

rlpA

Date:

2021-08-30

This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA.

Date:

2021-07-23