Detail Information for IndEnz0002018549
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