TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.B.9.1.1









Fatty acid outer membrane porin. Gated by high affinity ligand (fatty acid) binding which causes conformational changes in the N-terminus that open up a channel for substrate diffusion (Lepore et al., 2011).  May function in the transport of phenylpropanoids (resveratrol, naringenin and rutin) (Zhou et al. 2014).

Bacteria
Proteobacteria
FadL of E. coli
*1.B.9.1.2









FadL homologue (Bhat et al. 2011).

Bacteria
Proteobacteria
FadL homologue of Myxococcus xanthus
*1.B.9.1.3









Putative porin of 441 aas

Bacteria
Nitrospirae
Porin of Candidatus Nitrospira defluvii
*1.B.9.1.4









Outer membrane protein P1 of 459 aas

Bacteria
Proteobacteria
OmpP1 of Haemophilus influenzae
*1.B.9.1.5









Putative fatty acid-transporting porin of 434 aas, OmpP1, FadL, TodX.  It has used to generate an effective vaccine against Bordetella bronchiseptica (Zhang et al. 2019).

Bacteria
Proteobacteria
OmpP1 of Bordetella bronchiseptica (Alcaligenes bronchisepticus)
*1.B.9.1.6









Long alkane hydrocarbon chain (~C28) transporting outer membrane porin, FadL of 546 aas (Gregson et al. 2018).

Bacteria
Proteobacteria
FadL porin of the obligate marine hydrocarbon-degrading bacterium, Thalassolituus oleivorans MIL-1.
*1.B.9.2.1









Toluene/m-xylene outer membrane porin, XylN or FadL.  May also transport medium-chain-length 3-hydroxyalkanoic acids (Yuan et al. 2008).

Bacteria
Proteobacteria
XylN of Pseudomonas putida
*1.B.9.2.2









The 14 TMS hydrocarbon porin, TodX. The x-ray structure is known (3BS0-A) (Hearn et al., 2008).
Bacteria
Proteobacteria
TodX of Pseudomonas putida (3BS0_A)
*1.B.9.2.3









The 14 TMS hydrocarbon porin, TbuX. The crystal structure is known. (3BRY_A) (Hearn et al., 2008).
Bacteria
Proteobacteria
TbuX of Ralstonia pickettii (3BRY_A)(Q9RBW8)
*1.B.9.2.4









Putative aromatic hydrocarbon degradation pathway porin, FadL homologue, with an N-terminal transmembrane α-helix and about 16 putative β-TMSs.

Bacteria
Spirochaetes
FadL homologue of Treponema succinifaciens
*1.B.9.3.1









Salicylate ester (methyl and ethyl salicylates)/hydrocarbon outer membrane porin, SalD (Jones et al. 2000).

Bacteria
Proteobacteria
SalD of Acinetobacter sp. strain ADPI
*1.B.9.3.2









FadL homologue of 432 aas

Bacteria
Chlamydiae/Verrucomicrobia group
FadL of Parachlamydia acanthamoebae
*1.B.9.3.3









FadL homologue of 468 aas

Bacteria
Spirochaetes
FadL homologue of Leptospira interrogans
*1.B.9.4.1









Putative hemin receptor of 479 aas and ~20 β-strand

Bacteria
Bacteroidetes/Chlorobi group
Hemin receptor of Riemerella anatipestifer
*1.B.9.4.2









Uncharacterized porin of 542 aas

Bacteria
Bacteroidetes/Chlorobi group
UP of Prevotella oralis
*1.B.9.4.3









Putative porin of 543 aas

Bacteria
Bacteroidetes/Chlorobi group
Porin of Porphyromonas endodontalis
*1.B.9.4.4









Outer membrane protein transport protein (OmpP1/FadL/TodX family)

Bacteria
Bacteroidetes/Chlorobi group
OmpP1 of Saprospira grandis
*1.B.9.4.5









Membrane protein involved in aromatic hydrocarbon degradation of 481 aas
Bacteria
Caldithrix
OM porin of Caldithrix abyssi
*1.B.9.4.6









Uncharacterized protein of 472 aas
Bacteria
Bacteroidetes/Chlorobi group
UP of Ignavibacterium album
*1.B.9.4.7









Porin protein involved in aromatic hydrocarbon degradation; putative hemin receptor of 479 aas

Bacteria
Bacteroidetes/Chlorobi group
Putative porin of Pedobacter heparinus
*1.B.9.4.8









Uncharacterized membrane protein, predicted to be involved in aromatic hydrocarbon degradation; of 437 aas.

Bacteria
Planctomycetes
UP of planctomycete KSU-1