Protein Family Models

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

polysaccharide deacetylase family protein similar to Bacillus cereus peptidoglycan N-acetylglucosamine deacetylase which belongs to the Carbohydrate Esterase Family 4 (CE4)

Date:

2024-02-09

polysaccharide deacetylase family protein similar to Bacillus cereus peptidoglycan N-acetylglucosamine deacetylase which belongs to the Carbohydrate Esterase Family 4 (CE4)

Date:

2024-02-09

polysaccharide deacetylase family protein similar to Bacillus cereus peptidoglycan N-acetylglucosamine deacetylase which belongs to the Carbohydrate Esterase Family 4 (CE4)

Date:

2024-02-09

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

polysaccharide deacetylase family protein similar to Bacillus cereus peptidoglycan N-acetylglucosamine deacetylase which belongs to the Carbohydrate Esterase Family 4 (CE4)

Date:

2024-02-09

polysaccharide deacetylase family protein similar to Bacillus cereus peptidoglycan N-acetylglucosamine deacetylase which belongs to the Carbohydrate Esterase Family 4 (CE4)

Date:

2024-02-09

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Date:

2024-02-09

This domain represents the N-terminal domain of 6-phospho-N-acetylmuramidase (MupG) from Staphylococcus aureus [1], also found in putative phospho sugar glycosidases from Gram-negative and -positive species, but mainly firmicutes. MupG [1], specifically cleaves MurNAc 6P-GlcNAc, a product of cell wall turnover, into the sugars MurNAc 6P and GlcNAc, involved in cell wall turnover and recycling. Since some species, for example Lactobacillus plantarum, possess several putative paralogs, the substrate specificity of the proteins containing this domain may not be limited to cell wall sugars, but may include phosphorylated disaccharides in general. Most of these proteins appear to consist of two structural subdomains, as it can be seen in the two available crystal structures of Enterococcus faecalis (PDB:2p0o) and Bacillus cereus (PDB:1X7F). This entry is the larger N-terminal domain that constitutes a TIM-barrel like structure and the C-terminal domain is similar to the cyclophilin family. It should be noted that some proteins lack the C-terminal domain. [1]. 30524387. Recovery of the Peptidoglycan Turnover Product Released by the. Autolysin Atl in Staphylococcus aureus Involves the. Phosphotransferase System Transporter MurP and the Novel. 6-phospho-N-acetylmuramidase MupG.. Kluj RM, Ebner P, Adamek M, Ziemert N, Mayer C, Borisova M;. Front Microbiol. 2018;9:2725. (from Pfam)

Date:

2024-08-14

This family represents sublancin, a small bacteriocin active against Gram-positive bacteria. This family appears to be restricted to Bacilli. Sublancin was thought to be a lantibiotic but was later shown to be an S-linked glycopeptide [1,2]. Glycosylation is essential for its antimicrobial activity. Sublancin is biosynthesised as a precursor peptide bearing an N-terminal leader peptide, and a C-terminal core peptide that is converted into the mature peptide [1]. Sublancin comprises two alpha helices and a well-defined inter-helical loop [3]. Sublancin inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells and inhibits B.subtilis strain ATCC6633 and B. megaterium strain 14581 [2]. [1]. 21196935. Sublancin is not a lantibiotic but an S-linked glycopeptide.. Oman TJ, Boettcher JM, Wang H, Okalibe XN, van der Donk WA;. Nat Chem Biol. 2011;7:78-80.. [2]. 9722542. Identification and characterization of the structural and. transporter genes for, and the chemical and biological. properties of, sublancin 168, a novel lantibiotic produced by. Bacillus subtilis 168.. Paik SH, Chakicherla A, Hansen JN;. J Biol Chem. 1998;273:23134-23142.. [3]. 24405370. NMR structure of the S-linked glycopeptide sublancin 168.. Garcia De Gonzalo CV, Zhu L, Oman TJ, van der Donk WA;. ACS Chem Biol. 2014;9:796-801. (from Pfam)

Date:

2024-08-14

This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0000320) is described by MIBiG as an example of the following biosynthetic class, NRP (non-ribosomal peptide). This family includes a protein from the cereulide biosynthetic gene cluster from Bacillus cereus and appears to be predominantly found in Bacilli [1,2]. [1]. 15640177. Identification and partial characterization of the nonribosomal. peptide synthetase gene responsible for cereulide production in. emetic Bacillus cereus.. Ehling-Schulz M, Vukov N, Schulz A, Shaheen R, Andersson M,. Martlbauer E, Scherer S;. Appl Environ Microbiol. 2005;71:105-113.. [2]. 16512902. Cereulide synthetase gene cluster from emetic Bacillus cereus:. structure and location on a mega virulence plasmid related to. Bacillus anthracis toxin plasmid pXO1.. Ehling-Schulz M, Fricker M, Grallert H, Rieck P, Wagner M,. Scherer S;. BMC Microbiol. 2006;6:20. (from Pfam)

Date:

2024-08-14

This entry represents the N-terminal domain of BREX system Lon protease-like protein BrxL from Bacillus cereus and similar proteins. BrxL is part of a type 1 BREX system, which contains a C-terminal Lon-like protease domain (Pfam:PF05362). BREX systems (bacteriophage exclusion) provide immunity against bacteriophage, a system that allows phage adsorption but prevents phage DNA replication, without degradation of the phage DNA [1]. [1]. 25452498. BREX is a novel phage resistance system widespread in microbial. genomes.. Goldfarb T, Sberro H, Weinstock E, Cohen O, Doron S,. Charpak-Amikam Y, Afik S, Ofir G, Sorek R;. EMBO J. 2015;34:169-183. (from Pfam)

Date:

2024-08-14

This is the first of two N-terminal bacterial SH3 (SH3b) domains found in bacterial dipeptidyl-peptidases VI such as gamma-D-glutamyl-L-diamino acid endopeptidases. The first SH3b domain plays an important role in defining substrate specificity by contributing to the formation of the active site, such that only murein peptides with a free N-terminal alanine are allowed [1]. [1]. 20944232. Structure of the gamma-D-glutamyl-L-diamino acid endopeptidase. YkfC from Bacillus cereus in complex with L-Ala-gamma-D-Glu:. insights into substrate recognition by NlpC/P60 cysteine. peptidases.. Xu Q, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, Cai X,. Carlton D, Chen C, Chiu HJ, Chiu M, Clayton T, Das D, Deller MC,. Duan L, Ellrott K, Farr CL, Feuerhelm J, Grant JC, Grzechnik A,. Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P,. Krishna SS, Kumar A, Lam WW, Marciano D, Miller MD, Morse AT,. Nigoghossian E, Nopakun A, Okach L, Puckett C, Reyes R, Tien HJ,. Trame CB, van den Bedem H, Weekes D, Wooten T, Yeh A, Hodgson. KO, Wooley J, Elsliger MA, Deacon AM, Godzik A, Lesley SA,. Wilson IA;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:1354-1364. (from Pfam)

Date:

2024-08-14

This entry represents the ATPase domain found in BREX system Lon protease-like protein BrxL from Bacillus cereus and similar proteins. BrxL is part of a type 1 BREX system which contains a C-terminal Lon-like protease domain (Pfam:PF05362. BREX systems (bacteriophage exclusion) provide immunity against bacteriophage, a system that allows phage adsorption but prevents phage DNA replication, without degradation of the phage DNA [1]. Methylation of bacterial DNA by PglX probably guides self/non-self discrimination. This entry also includes a few uncharacterised viral sequences. [1]. 25452498. BREX is a novel phage resistance system widespread in microbial. genomes.. Goldfarb T, Sberro H, Weinstock E, Cohen O, Doron S,. Charpak-Amikam Y, Afik S, Ofir G, Sorek R;. EMBO J. 2015;34:169-183. (from Pfam)

Date:

2024-08-14

This domain is found in a prophage protein BC1872 found in B. cereus. The domain forms a three-layer beta/alpha/beta sandwich. Three alpha-helices, alpha1, alpha2, and alpha3, are sandwiched on one side by three-stranded antiparallel beta-sheet (beta3, beta4, and beta5) and on the other by a beta-hairpin (beta1 and beta2) [1]. [1]. 16596646. Structure of phage protein BC1872 from Bacillus cereus, a. singleton with new fold.. Zhang R, Joachimiak G, Jiang S, Cipriani A, Collart F,. Joachimiak A;. Proteins. 2006;64:280-283. (from Pfam)

Date:

2024-08-14

This family consists of uncharacterized proteins around 270 residues in length and is mainly found in various Bacillus cereus species. Some members of this family are annotated as Galactose-1-phosphate uridylyltransferases, but the specific function of this family is unknown. (from Pfam)

Date:

2024-08-14

This family consists of uncharacterized proteins around 170 residues in length and is mainly found in various Bacillus species (B. cereus, B. thuringiensis and B. anthracis). The solved structure of B. anthracis homologs has a variant of the Greek-key beta barrel fold, making the DUF4870 family a member of a large group of bacterial immunoglobulin like domains, but the functional consequences of this classification remain unknown. (from Pfam)

Date:

2024-08-14