Protein Family Models

Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence [1]. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a 'handle' domain made up of four (N lobe) or eight (C lobe) beta strands [2]. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf [3]. The 4-residue conserved LSAC motif found at the amino terminus of TbpB represents a prototypical lipobox, with the cysteine residue serving as the first amino acid in the mature protein which is subsequently modified by the addition of a diacyl glycerol. A second conserved motif of interest is located two amino acids downstream of the LSAC site. This region consists of four glycine residues in tan. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

Bacterial lipoproteins represent a large group of specialised membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence [1]. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialised uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a 'handle' domain made up of four (N lobe) or eight (C lobe) beta strands [2]. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf [3]. This domain family is found in the handle domain of the C lobe (domain C) of TbpB proteins. It consists of a squashed six-stranded beta sheet flanked by two antiparallel beta strands and has no supporting alpha helix as in the N lobe [2]. [1]. 18186471. The solution structure of the outer membrane lipoprotein OmlA. from Xanthomonas axonopodis pv. citri reveals a protein fold. implicated in protein. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

The mediator complex is part of the RNA polymerase II holoenzyme. Rox3 is a subunit of the mediator complex. [1]. 11383511. Yeast nuclear extract contains two major forms of RNA polymerase. II mediator complexes.. Liu Y, Ranish JA, Aebersold R, Hahn S;. J Biol Chem. 2001;276:7169-7175. (from Pfam)

Date:

2024-08-14

Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence [1]. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a "handle" domain made up of four (N lobe) or eight (C lobe) beta strands [2]. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf [3]. This domain family is found in C and N lobe eight stranded beta barrel region of TbpB proteins. The eight-stranded barrel domains in N and C lobe draw comparisons to eight-stranded beta barrel outer-membrane protein W (OmpW). However, the barrel domains of TbpB have the hydrophobic residues line the inner surface of the beta barrels to create a stable hydrophobic core [2]. [1]. 18186471. The solut. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

ligand-gated channel protein similar to Vibrio cholerae iron-regulated outer membrane virulence protein, which is involved in the initial step of iron uptake by binding ferric vibriobactin, an iron chelatin siderophore that allows V.cholerae to extract iron from the environment

Date:

2021-02-01

HarA is a heme-binding NEAT-domain (NEAr Transporter, PF05031) protein which has been shown to bind to the haptoglobin-hemoglobin complex in order to extract heme from it. HarA has also been reported to bind hemoglobin directly [2]. HarA (also known as IsdH) contains three NEAT domains as well as a sortase A C-terminal signal for localization to the cell wall. The heme bound at the third of these NEAT domains has been shown to be transferred to the IsdA protein also localized at the cell wall, presumably through an additional specific protein-protein interaction [3]. Haptoglobin is a hemoglobin carrier protein involved in scavenging hemoglobin in the blood following red blood cell lysis and targetting it to the liver.

Gene:

harA

Date:

2021-04-27