Table I.

E. coli OMP Substrates Used in the BAM Complex Studies^a

Substrate	UniProt ID	No. of β-strands	MW (kDa)	Oligomeric state	Function	PDB ID	Reference
OmpA	P0A910	8	37.2	Dimer	Porin and receptor	1BXW, 1G90, 1QJP, 2GE4, 2JMM	40
OmpT	P09169	10	35.6	Possible pentamerb	Protease	1I78	41
Ag43	P39180	12c	106.8	Monomerd	Autotransporter	(Unsolved)	42
AIDA-I	Q03155	12c	132.3	Monomerd	Autotransporter	(Unsolved)	43
Hbp	O88093	12	148.3	Monomerd	Autotransporter	1WXR, 3AEH, 3AK5	44
Intimin	P43261	12c	101.8	Dimer	Autotransporter	(β-Barrel unsolved)	45
Pet	O68900	12c	139.8	Monomerd	Autotransporter	(Unsolved)	42
TolC	P02930	12	53.7	Trimer	Transporter	1EK9, 1TQQ, 2VDD, 2VDE, 2WMZ, 2XMN	40
OmpC	P06996	16	40.4	Trimer	Porin	2J1N, 2J4U, 2XE1, 2XE2, 2XE3, 2XE5, 2XG6	40
OmpF	P02931	16	39.3	Trimer	Porin	1BT9, 1GFM, 1GFN, 1GFO, 1GFP, 1GFQ, 1HXT, 1HXU, 1HXX, 1MPF, 1OPF, 2OMF, 2ZFG, 2ZLD, 3FYX, 3HW9, 3HWB, 3K19, 3K1B, 3O0E	40
PhoE	P02932	16	38.9	Trimer	Porin	1PHO	36
LamB	P02943	18	49.9	Trimer	Porin	1AF6, 1MAL, 1MPM, 1MPN, 1MPO, 1MPQ	40
FimD	P30130	24	96.5	Dimer	Transporter	1ZDV, 1ZDX, 1ZE3, 3BWU, 3OHN, 3RFZ	46

^aThis table only lists E. coli OMPs that have been shown to require the BAM complex for correct assembly. Although not listed here, it should be noted that OMPs from other species of Gram-negative bacteria such as PilQ and PorA from N. meningitidis have been used in the functional studies of the BAM complex.⁴

^bGel filtration analysis of OmpT suggests possible pentamer formation.⁴⁷

^cBased on currently available structures, most autotransporters are predicted to have 12-stranded β-barrels.

^dThese proteins have been classified as monomeric proteins.⁴⁸