UniProt functional annotation for P76578



	UniProt functional annotation for P76578

UniProt code: P76578.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Protects the bacterial cell from host peptidases (PubMed:18697741, PubMed:26143919, PubMed:26100869). Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase (PubMed:26143919, PubMed:26100869). Trapped peptidases are still active except against very large substrates (PubMed:26100869). May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases (PubMed:26100869). {ECO:0000269|PubMed:18697741, ECO:0000269|PubMed:26100869, ECO:0000269|PubMed:26143919}.

Subunit: May form homooligomers. {ECO:0000269|PubMed:21210718}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18697741, ECO:0000269|PubMed:21210718}; Lipid-anchor {ECO:0000255|PROSITE- ProRule:PRU00303}; Periplasmic side {ECO:0000269|PubMed:18697741}.

Domain: Cleavage causes major structural rearrangement of more than half the 13-domain structure from a native to a compact induced form. {ECO:0000269|PubMed:26100869}.

Miscellaneous: Bacterial alpha-2-macroglobulins were probably acquired one or more times by horizontal gene transfer from metazoan hosts. {ECO:0000305|PubMed:15186489}.

Similarity: Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Protects the bacterial cell from host peptidases (PubMed:18697741, PubMed:26143919, PubMed:26100869). Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase (PubMed:26143919, PubMed:26100869). Trapped peptidases are still active except against very large substrates (PubMed:26100869). May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases (PubMed:26100869). {ECO:0000269\|PubMed:18697741, ECO:0000269\|PubMed:26100869, ECO:0000269\|PubMed:26143919}.


Subunit:		May form homooligomers. {ECO:0000269\|PubMed:21210718}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:18697741, ECO:0000269\|PubMed:21210718}; Lipid-anchor {ECO:0000255\|PROSITE- ProRule:PRU00303}; Periplasmic side {ECO:0000269\|PubMed:18697741}.
Domain:		Cleavage causes major structural rearrangement of more than half the 13-domain structure from a native to a compact induced form. {ECO:0000269\|PubMed:26100869}.
Miscellaneous:		Bacterial alpha-2-macroglobulins were probably acquired one or more times by horizontal gene transfer from metazoan hosts. {ECO:0000305\|PubMed:15186489}.
Similarity:		Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily. {ECO:0000305}.