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Links from Protein

Items: 7

1.

M56 family metallopeptidase

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
Family Accession:
NF017390.5
Method:
HMM
2.

M48 family metalloprotease

Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologues such as Human FACE-1 protease. These are metallopeptidases, with the characteristic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit [1,2]. [1]. 23539602. Structure of the integral membrane protein CAAX protease Ste24p. Pryor EE Jr, Horanyi PS, Clark KM, Fedoriw N, Connelly SM, Koszelak-Rosenblum M, Zhu G, Malkowski MG, Wiener MC, Dumont ME;. Science. 2013;339:1600-1604. [2]. 23539603. The structural basis of ZMPSTE24-dependent laminopathies. Quigley A, Dong YY, Pike AC, Dong L, Shrestha L, Berridge G, Stansfeld PJ, Sansom MS, Edwards AM, Bountra C, von Delft F, Bullock AN, Burgess-Brown NA, Carpenter EP;. Science. 2013;339:1604-1607. (from Pfam)

GO Terms:
Molecular Function:
metalloendopeptidase activity (GO:0004222)
Biological Process:
proteolysis (GO:0006508)
Date:
2024-10-16
Family Accession:
NF013594.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

MecR1 family protein

MecR1 family protein

Date:
2017-03-02
Family Accession:
11467994
Method:
Sparcle
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