IED ID | IndEnz0002018549 |
Enzyme Type ID | protease018549 |
Protein Name |
Alpha-2-macroglobulin ECAM |
Gene Name | yfhM b2520 JW2504 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MKKLRVAACMLMLALAGCDNNDNAPTAVKKDAPSEVTKAASSENASSAKLSVPERQKLAQQSAGKVLTLLDLSEVQLDGAATLVLTFSIPLDPDQDFSRVIHVVDKKSGKVDGAWELSDNLKELRLRHLEPKRDLIVTIGKEVKALNNATFSKDYEKTITTRDIQPSVGFASRGSLLPGKVVEGLPVMALNVNNVDVNFFRVKPESLPAFISQWEYRNSLANWQSDKLLQMADLVYTGRFDLNPARNTREKLLLPLGDIKPLQQAGVYLAVMNQAGRYDYSNPATLFTLSDIGVSAHRYHNRLDIFTQSLENGAAQQGIEVSLLNEKGQTLTQATSDAQGHVQLENDKNAALLLARKDGQTTLLDLKLPALDLAEFNIAGAPGYSKQFFMFGPRDLYRPGETVILNGLLRDADGKALPNQPIKLDVIKPDGQVLRSVVSQPENGLYHFTWPLDSNAATGMWHIRANTGDNQYRMWDFHVEDFMPERMALNLTGEKTPLTPKDEVKFSVVGYYLYGAPANGNTLQGQLFLRPLREAVSALPGFEFGDIAAENLSRTLDEVQLTLDDKGRGEVSTESQWKETHSPLQVIFQGSLLESGGRPVTRRAEQAIWPADALPGIRPQFASKSVYDYRTDSTVKQPIVDEGSNAAFDIVYSDAQGVKKAVSGLQVRLIRERRDYYWNWSEDEGWQSQFDQKDLIENEQTLDLKADETGKVSFPVEWGAYRLEVKAPNEAVSSVRFWAGYSWQDNSDGSGAVRPDRVTLKLDKASYRPGDTIKLHIAAPTAGKGYAMVESSEGPLWWQEIDVRAQGLDLTIPVDKTWNRHDLYLSTLVVRPGDKSRSATPKRAVGVLHLPLGDENRRLDLALETPAKMRPNQPLTVKIKASTKNGEKPKQVNVLVSAVDSGVLNITDYVTPDPWQAFFGQKRYGADIYDIYGQVIEGQGRLAALRFGGDGDELKRGGKPPVNHVNIVVQQALPVTLNEQGEGSVTLPIGDFNGELRVMAQAWTADDFGSNESKVIVAAPVIAELNMPRFMASGDTSRLTLDITNLTDKPQKLNVALTASGLLELVSDSPAAVELAPGVRTTLFIPVRALPGYGDGEIQATISGLALPGETVADQHKQWKIGVRPAFPAQTVNYGTALQPGETWAIPADGLQNFSPVTLEGQLLLSGKPPLNIARYIKELKAYPYGCLEQTASGLFPSLYTNAAQLQALGIKGDSDEKRRASVDIGISRLLQMQRDNGGFALWDKNGDEEYWLTAYVMDFLVRAGEQGYSVPTDAINRGNERLLRYLQDPGMMSIPYADNLKASKFAVQSYAALVLARQQKAPLGALREIWEHRADAASGLPLLQLGVALKTMGDATRGEEAIALALKTPRNSDERIWLGDYGSSLRDNALMLSLLEENKLLPDEQYTLLNTLSQQAFGERWLSTQESNALFLAARTIQDLPGKWQAQTSFSAEQLTGEKAQNSNLNSDQLVTLQVSNSGDQPLWLRMDASGYPQSAPLPANNVLQIERHILGTDGKSKSLDSLRSGDLVLVWLQVKASNSVPDALVVDLLPAGLELENQNLANGSASLEQSGGEVQNLLNQMQQASIKHIEFRDDRFVAAVAVDEYQPVTLVYLARAVTPGTYQVPQPMVESMYVPQWRATGAAEDLLIVRP |
Enzyme Length | 1653 |
Uniprot Accession Number | P76578 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | 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}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (102); Chain (1); Coiled coil (1); Cross-link (1); Helix (32); Lipidation (2); Signal peptide (1); Turn (14) |
Keywords | 3D-structure;Cell inner membrane;Cell membrane;Coiled coil;Lipoprotein;Membrane;Palmitate;Protease inhibitor;Reference proteome;Signal;Thioester bond |
Interact With | |
Induction | |
Subcellular Location | 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}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
Structure 3D | Electron microscopy (1); X-ray crystallography (5) |
Cross Reference PDB | 4RTD; 4ZIQ; 4ZIU; 4ZJG; 4ZJH; 5A42; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 181,585 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |