Protein Family Models

Production of beta-Lactamase and penicillin-binding protein 2a (which mediate staphylococcal resistance to beta-lactam antibiotics) is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. Homologues to this peptidase domain, which corresponds to Merops family M56, are also found in a number of other bacterial genome sequences. [1]. 11245199. Microbiology. Signaling antibiotic resistance in staphylococci. Archer GL, Bosilevac JM;. Science 2001;291:1915-1916. [2]. 11239156. A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci. Zhang HZ, Hackbarth CJ, Chansky KM, Chambers HF;. Science 2001;291:1962-1965. [3]. 9164468. Mechanisms of methicillin resistance in staphylococci. Brakstad OG, Maeland JA;. APMIS 1997;105:264-276. [4]. 23733187. A novel family of soluble minimal scaffolds provides structural insight into the catalytic domains of integral membrane metallopeptidases. Lopez-Pelegrin M, Cerda-Costa N, Martinez-Jimenez F, Cintas-Pedrola A, Canals A, Peinado JR, Marti-Renom MA, Lopez-Otin C, Arolas JL, Gomis-Ruth FX;. J Biol Chem. 2013;288:21279-21294. (from Pfam)

Date:

2024-10-16

The TonB_C domain is the well-characterised C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane [1]. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance [2]. [1]. 16741124. Outer membrane active transport: structure of the BtuB:TonB complex. Shultis DD, Purdy MD, Banchs CN, Wiener MC;. Science. 2006;312:1396-1399. [2]. 21277822. Recent insights into iron import by bacteria. Braun V, Hantke K;. Curr Opin Chem Biol. 2011;15:328-334. (from Pfam)

Date:

2024-10-16

This HMM represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm.

Date:

2021-05-12

MecR1 family protein

Date:

2017-03-02