UniProt functional annotation for P0A903



	UniProt functional annotation for P0A903

UniProt code: P0A903.

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. 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:20378773, 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 BamD and BamE. 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: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_00924, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00924, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27686148}.

Domain: Contains two well-defined domains connected by a flexible linker. The C-terminal domain may serve as an important protein-binding surface for interaction with other Bam components or substrates. In addition, contains a long unstructured N-terminal region, which is required to stabilize the BamCD complex. Only the N-terminus of this protein is observed in the Bam complex in X-ray or EM structures, most of the protein must be highly mobile (PubMed:26900875, PubMed:26901871, PubMed:27686148, PubMed:26744406). {ECO:0000269|PubMed:21624375, ECO:0000269|PubMed:21937441, ECO:0000269|PubMed:22102230, ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.

Mass spectrometry: Mass=35163; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Mass spectrometry: Mass=35183; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269|PubMed:27686148};

Similarity: Belongs to the BamC family. {ECO:0000255|HAMAP- Rule:MF_00924}.

Sequence caution: Sequence=M33928; Type=Frameshift; 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. 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:20378773, 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 BamD and BamE. 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: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_00924, ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871}; Lipid-anchor {ECO:0000255\|HAMAP-Rule:MF_00924, ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:27686148}.
Domain:		Contains two well-defined domains connected by a flexible linker. The C-terminal domain may serve as an important protein-binding surface for interaction with other Bam components or substrates. In addition, contains a long unstructured N-terminal region, which is required to stabilize the BamCD complex. Only the N-terminus of this protein is observed in the Bam complex in X-ray or EM structures, most of the protein must be highly mobile (PubMed:26900875, PubMed:26901871, PubMed:27686148, PubMed:26744406). {ECO:0000269\|PubMed:21624375, ECO:0000269\|PubMed:21937441, ECO:0000269\|PubMed:22102230, ECO:0000269\|PubMed:26744406, ECO:0000269\|PubMed:26900875, ECO:0000269\|PubMed:26901871, ECO:0000269\|PubMed:27686148}.
Mass spectrometry:		Mass=35163; Method=Electrospray; Note=With 3 palmitic acid (C16) acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Mass spectrometry:		Mass=35183; Method=Electrospray; Note=With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.; Evidence={ECO:0000269\|PubMed:27686148};
Similarity:		Belongs to the BamC family. {ECO:0000255\|HAMAP- Rule:MF_00924}.
Sequence caution:		Sequence=M33928; Type=Frameshift; Evidence={ECO:0000305};