Summary: BlaR1 peptidase M56
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BlaR1 peptidase M56 Provide feedback
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.
Zhang HZ, Hackbarth CJ, Chansky KM, Chambers HF; , Science 2001;291:1962-1965.: A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci. PUBMED:11239156 EPMC:11239156
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.: A novel family of soluble minimal scaffolds provides structural insight into the catalytic domains of integral membrane metallopeptidases. PUBMED:23733187 EPMC:23733187
Internal database links
|SCOOP:||DUF955 WLM DUF2268 DUF4157 DUF4538 Peptidase_M48_N|
|Similarity to PfamA using HHSearch:||Peptidase_M48|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008756
This domain is found in a group of metallopeptidases belonging to MEROPS peptidase family M56 (clan M-). The predicted active site residues for members of this family occur in the motif HEXXH. The type example is BlaR1 peptidase from Bacillus licheniformis.
BlaR1 is a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis [PUBMED:2404938].
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Clan MA is one of two zinc-dependent metallopeptidases that contain the HEXXH motif. The two histidines are zinc ligands. The structures of this clan show the active site is between its two sub-domains.
The clan contains the following 58 members:Aspzincin_M35 Astacin BSP DUF1570 DUF2201_N DUF2268 DUF3152 DUF3267 DUF3633 DUF3810 DUF4157 DUF4344 DUF45 DUF4953 DUF955 HRXXH Peptidase_M1 Peptidase_M10 Peptidase_M11 Peptidase_M13 Peptidase_M2 Peptidase_M27 Peptidase_M3 Peptidase_M30 Peptidase_M32 Peptidase_M35 Peptidase_M36 Peptidase_M4 Peptidase_M41 Peptidase_M43 Peptidase_M48 Peptidase_M4_C Peptidase_M50 Peptidase_M50B Peptidase_M54 Peptidase_M56 Peptidase_M57 Peptidase_M6 Peptidase_M60 Peptidase_M61 Peptidase_M64 Peptidase_M66 Peptidase_M7 Peptidase_M8 Peptidase_M9 Peptidase_M91 Peptidase_Mx Peptidase_Mx1 Peptidase_U49 Reprolysin Reprolysin_2 Reprolysin_3 Reprolysin_4 Reprolysin_5 SprT-like WLM Zn_peptidase Zn_peptidase_2
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Curation and family details
|Number in seed:||12|
|Number in full:||844|
|Average length of the domain:||236.30 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||42.17 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Peptidase_M56 domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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