UniProt functional annotation for P0AC02



	UniProt functional annotation for P0AC02

UniProt code: P0AC02.

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. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. 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:16824102, ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:22281737, 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 BamE. Interacts directly with BamA. 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). {ECO:0000269|PubMed:15851030, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16824102, ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:21937441, ECO:0000269|PubMed:22281737, 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_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27686148}.

Domain: The N-terminal may interact with various proteins as a chaperone to assist in the folding and insertion of proteins into the outer membrane. The C-terminal region may serve as the link between BamA, BamC and BamE. {ECO:0000269|PubMed:22281737}.

Mass spectrometry: Mass=26582; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Mass spectrometry: Mass=26603; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Disruption phenotype: Depletion decreases the density of outer membrane proteins, but does not significantly affect transport of lipopolysaccharides to the outer membrane. {ECO:0000269|PubMed:16824102}.

Similarity: Belongs to the BamD family. {ECO:0000255|HAMAP- Rule:MF_00922}.

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. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. 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:16824102, ECO:0000269\|PubMed:20378773, ECO:0000269\|PubMed:21586578, ECO:0000269\|PubMed:21823654, ECO:0000269\|PubMed:22281737, 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 BamE. Interacts directly with BamA. 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). {ECO:0000269\|PubMed:15851030, ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:16824102, ECO:0000269\|PubMed:20378773, ECO:0000269\|PubMed:21586578, ECO:0000269\|PubMed:21823654, ECO:0000269\|PubMed:21937441, ECO:0000269\|PubMed:22281737, 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_00922, ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871}; Lipid-anchor {ECO:0000255\|HAMAP-Rule:MF_00922, ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:27686148}.
Domain:		The N-terminal may interact with various proteins as a chaperone to assist in the folding and insertion of proteins into the outer membrane. The C-terminal region may serve as the link between BamA, BamC and BamE. {ECO:0000269\|PubMed:22281737}.
Mass spectrometry:		Mass=26582; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Mass spectrometry:		Mass=26603; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Disruption phenotype:		Depletion decreases the density of outer membrane proteins, but does not significantly affect transport of lipopolysaccharides to the outer membrane. {ECO:0000269\|PubMed:16824102}.
Similarity:		Belongs to the BamD family. {ECO:0000255\|HAMAP- Rule:MF_00922}.