| IED ID | IndEnz0002018537 |
| Enzyme Type ID | protease018537 |
| Protein Name |
Outer membrane protein assembly factor BamA Omp85 |
| Gene Name | bamA yaeT yzzN yzzY b0177 JW0172 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYAELSVTNPYFTVDGVSLGGRLFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNSLRAGLGYVHNSLSNMQPQVAMWRYLYSMGEHPSTSDQDNSFKTDDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVTLDTATYVPIDDDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPHQASNYDPDYDYECATQDGAKDLCKSDDAVGGNAMAVASLEFITPTPFISDKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW |
| Enzyme Length | 810 |
| Uniprot Accession Number | P0A940 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406). {ECO:0000269|PubMed:15951436, ECO:0000269|PubMed:16102012, ECO:0000269|PubMed:16824102, ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.; FUNCTION: (Microbial infection) Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components (PubMed:18761695). Is not the receptor for CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93; the decreased expression of bamA101 in some experiments decreases the level of outer membrane proteins in general (PubMed:23469034, PubMed:23882017). Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC (PubMed:23882017). {ECO:0000269|PubMed:18761695, ECO:0000269|PubMed:23469034, ECO:0000269|PubMed:23882017}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (50); Chain (1); Domain (5); Helix (17); Mutagenesis (31); Sequence conflict (5); Signal peptide (1); Topological domain (16); Transmembrane (16); Turn (11) |
| Keywords | 3D-structure;Cell adhesion;Cell outer membrane;Direct protein sequencing;Membrane;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane beta strand |
| Interact With | P77774; P0AC02; P69411 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01430, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24619089, ECO:0000269|PubMed:24914988, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:9298646}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence="ECO:0000255|HAMAP-Rule:MF_01430, ECO:0000269|PubMed:9298646" |
| Structure 3D | NMR spectroscopy (1); Electron microscopy (25); X-ray crystallography (17) |
| Cross Reference PDB | 2QCZ; 2QDF; 2V9H; 3EFC; 3OG5; 3Q6B; 4C4V; 4N75; 4PK1; 4XGA; 5AYW; 5D0O; 5D0Q; 5EKQ; 5LJO; 6LYQ; 6LYR; 6LYS; 6LYU; 6SMX; 6SN0; 6SN2; 6SN3; 6SN4; 6SN5; 6SN7; 6SN8; 6SN9; 6SO7; 6SO8; 6SOA; 6SOB; 6SOC; 6SOG; 6SOH; 6SOJ; 6T1W; 6V05; 7BNQ; 7NBX; 7NCS; 7ND0; 7NRI; |
| Mapped Pubmed ID | 16556215; 16606699; 16858726; 17088246; 17214547; 17542925; 18165306; 21070948; 22178970; 22544271; 22753067; 22948914; 25468906; 25525882; 26894671; 32528179; 32572278; 33368572; 33854236; 34234105; |
| Motif | |
| Gene Encoded By | |
| Mass | 90,553 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |