Protein Family Models

This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins. Paper describing PDB structure 3h94. This domain is unresolved. [1]. 19695261. Crystal structure of the membrane fusion protein CusB from. Escherichia coli.. Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK,. Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW;. J Mol Biol. 2009;393:342-355.. Paper describing PDB structure 3ne5. This domain is unresolved.. [2]. 21350490. Crystal structure of the CusBA heavy-metal efflux complex of. Escherichia coli.. Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, Yu. EW;. Nature. 2011;470:558-562.. Paper describing PDB structure 3rfu. This domain is unresolved.. [3]. 21716286. Crystal structure of a copper-transporting PIB-type ATPase.. Gourdon P, Liu XY, Skjorringe T, Morth JP, Moller LB, Pedersen. BP, Nissen P;. Nature. 2011;475:59-64.. Paper describing PDB structure 4bbj. This domain is unresolved.. [4]. 24317491. Copper-transporting P-type ATPases use a unique ion-release. pathway.. Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller. LB, White SH, Nissen P, Gourdon P;. Nat Struct Mol Biol. 2014;21:43-48. (from Pfam)

Date:

2024-08-14

HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons. [1]. 19695261. Crystal structure of the membrane fusion protein CusB from. Escherichia coli.. Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK,. Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW;. J Mol Biol. 2009;393:342-355. (from Pfam)

Date:

2024-08-14

HlyD_D4 is the long alpha-hairpin domain in the centre of CusB or HlyD proteins. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons. HlyD_D4 is thought to interact with the alpha-helical tunnels of the corresponding outer-membrane channels, ie the periplasmic domain of CusC [1]. [1]. 19695261. Crystal structure of the membrane fusion protein CusB from. Escherichia coli.. Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK,. Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW;. J Mol Biol. 2009;393:342-355. (from Pfam)

Date:

2024-08-14

This is a family of largely bacterial haemolysin translocator HlyD proteins. (from Pfam)

Date:

2024-08-14

This HMM represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of PF00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that HMM. The related HlyD secretion protein, for which PF00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane.

Date:

2024-06-14