UniProt functional annotation for P0A937



	UniProt functional annotation for P0A937

UniProt code: P0A937.

Organism: Escherichia coli (strain K12).

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

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. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD. 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:17404237, ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21207987, ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:22178970, ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.

Subunit: Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Forms a subcomplex with BamC and BamD. Monomer in the periplasm, but is able to adopt a dimeric conformation in the cytoplasm (PubMed:21207987). The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406). The intact Bam complex can have 2 BamE subunits (PubMed:27686148). {ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21139201, ECO:0000269|PubMed:21207987, ECO:0000269|PubMed:21212804, ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.

Subcellular location: Cell outer membrane {ECO:0000255|HAMAP- Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:27686148}.

Mass spectrometry: Mass=12383; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Mass spectrometry: Mass=12413; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Disruption phenotype: Mutants show minor defects in the assembly of outer membrane proteins. {ECO:0000269|PubMed:17404237}.

Similarity: Belongs to the BamE family. {ECO:0000255|HAMAP- Rule:MF_00925}.

Sequence caution: Sequence=CAA36847.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown provenance, it does not match this entry.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


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



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. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD. 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:17404237, ECO:0000269\|PubMed:20378773, ECO:0000269\|PubMed:21207987, ECO:0000269\|PubMed:21586578, ECO:0000269\|PubMed:21823654, ECO:0000269\|PubMed:22178970, ECO:0000269\|PubMed:26744406, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871, ECO:0000269\|PubMed:27686148}.


Subunit:		Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Forms a subcomplex with BamC and BamD. Monomer in the periplasm, but is able to adopt a dimeric conformation in the cytoplasm (PubMed:21207987). The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406). The intact Bam complex can have 2 BamE subunits (PubMed:27686148). {ECO:0000269\|PubMed:17404237, ECO:0000269\|PubMed:20378773, ECO:0000269\|PubMed:21139201, ECO:0000269\|PubMed:21207987, ECO:0000269\|PubMed:21212804, ECO:0000269\|PubMed:21586578, ECO:0000269\|PubMed:21823654, ECO:0000269\|PubMed:26744406, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871, ECO:0000269\|PubMed:27686148}.
Subcellular location:		Cell outer membrane {ECO:0000255\|HAMAP- Rule:MF_00925, ECO:0000269\|PubMed:17404237, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871}; Lipid-anchor {ECO:0000255\|HAMAP-Rule:MF_00925, ECO:0000269\|PubMed:17404237, ECO:0000269\|PubMed:27686148}.
Mass spectrometry:		Mass=12383; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Mass spectrometry:		Mass=12413; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Disruption phenotype:		Mutants show minor defects in the assembly of outer membrane proteins. {ECO:0000269\|PubMed:17404237}.
Similarity:		Belongs to the BamE family. {ECO:0000255\|HAMAP- Rule:MF_00925}.
Sequence caution:		Sequence=CAA36847.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown provenance, it does not match this entry.; Evidence={ECO:0000305};