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TCID	Name	Domain	Kingdom/Phylum	Protein(s)
1.B.25.1.1	OprD2; OccD1; porin D transports cationic amino acids, peptides and other compounds: lysine, arginine, histidine, ornithine, basic di- and tri-peptides, and cationic antibiotics such as imipenem (n-formimidoylthienamycin) and other penems and carbapenems (Tamber et al., 2006). The 3-d structure and drugs transported are known (4FOZ; Parkin and Khalid 2014). OprD is the vitronectin receptor. Vitronectin enhances P. aeruginosa adhesion to host epithelial cells and thereby enhances virulence (Paulsson et al. 2015). Loss promotes carbapenem resistance (Shen and Fang 2015; Cavalcanti et al. 2015). Loss results in resistance to meropenem (Fluit et al. 2019). Carbapenem resistance in difficult-to-treat P. aeruginosa strains can be mediated by loss or reduction of the OprD porin (Do Rego and Timsit 2023).	Bacteria	Pseudomonadota	OprD2 of Pseudomonas aeruginosa (P32722)
1.B.25.1.2	OprE1 (OprE; OccK8) porin (anaerobically induced). May participate in chromate resistance (Rivera et al., 2008). The high-resolution X-ray structure and electrophysiology highlight a very narrow pore. However, transport of natural amino acids and antibiotics, among them ceftazidime, has been demonstrated (Samanta et al. 2018). As in general porins, the internal electric field favors the translocation of polar molecules by gainful energy compensation in the central constriction region. The comparatively narrow pore can undergo a substrate-induced expansion to accommodate relatively large-sized substrates (Samanta et al. 2018).	Bacteria	Pseudomonadota	OprE1 of Pseudomonas aeruginosa (Q51510)
1.B.25.1.3	OprE3 (OprQ) porin (Okamoto et al. 1999).	Bacteria	Pseudomonadota	OprE3 of Pseudomonas aeruginosa (O24779)
1.B.25.1.4	PhaK phenylacetate/organic acid porin	Bacteria	Pseudomonadota	PhaK of Pseudomonas putida (O84986)
1.B.25.1.5	GusC (UidC) putative glucuronide porin (Liang et al., 2005). Reported to enhance the activity of the UidB (GusB) glucuronide transporter (TC# 2.A.2.1.5). Glucuronide transport does not occur in strain K12 due to a variant at position 100 of the UidB protein.	Bacteria	Pseudomonadota	GusC of E. coli (Q47706)
1.B.25.1.6	Vanillate trafficing porin, VanP. 85% identical to OprD of Acinetobacter baumannii which when mutated confers MDR (Yang et al. 2015).	Bacteria	Pseudomonadota	VanP of Acinetobacter sp. ADP1 (Q6FDI3)
1.B.25.1.7	OpdO pyroglutamate-specific porin (Tamber et al., 2006)	Bacteria	Pseudomonadota	OpdO of Pseudomonas aeruginosa (AAG05501)
1.B.25.1.8	Anion-selective OpdK (OccK1 or OpdK) benzoate/vanillate-selective porin (Tamber et al., 2006; Eren et al., 2012; Liu et al. 2012). The structure of the OpdK porin, specific for vanillate and related small aromatic acids, has been solved by x-ray crystallography (3SYS_A). It is a labile trimer with monomers of an 18 β-stranded barrel and with an inner diameter of 8Å (Biswas et al., 2008). Other substrates transported (but less well) include 4-nitrobenzoate, caproate, octanoate, carbenicillin, cefoxitin, tetracycline antibiotics, and carbapenem antibioitics (imipenem and meropenem) (Eren et al., 2012). Molecular dynamic simulations and mutant analyses have been reported (Wang et al. 2012).	Bacteria	Pseudomonadota	OpdK of Pseudomonas aeruginosa (AAG08283)
1.B.25.1.9	OpdP glycine-glutamate-selective porin (Tamber et al., 2006)	Bacteria	Pseudomonadota	OpdP of Pseudomonas aeruginosa (AAG07889)
1.B.25.1.10	A tricarboxylate transporting porin, OdpH (Occk5) induced by and transports cis-aconitate, isocitrate and citrate; exhibits a large single channel conductance (Tamber et al., 2006; 2007). This porin exhibits a high degree of anion selectivity, and the outer core and O-antigens of LPS sterically occlude the channel entrance to decrease the diffusion constants of approaching ions (Lee et al. 2018).	Bacteria	Pseudomonadota	OpdH of Pseudomonas aeruginosa (AAG04144)
1.B.25.1.11	OpdB proline-selective porin (Tamber et al., 2006)	Bacteria	Pseudomonadota	OpdB of Pseudomonas aeruginosa (AAG06088)
1.B.25.1.12	OpdC or OccD2 histidine-selective porin (Tamber et al., 2006). The 3-D structure and substrate spcificities are known (PDB 3SY9; Eren et al. 2012).	Bacteria	Pseudomonadota	OpdC of Pseudomonas aeruginosa (AAG03552)
1.B.25.1.13	Chitoporin, ChiP or YbfM of 468 aas. Takes up chitosugars such as chitobiose. It also plays a role in carbapenem (imipenem) resistance. The orthologue in Proteus mirabilis is ImpR, and that in Salmonella species is YbfM. It is subject to regulation by the small RNA, MicM (Tsai et al. 2015). Loss of OmpC and OmpF results in poor growth, by expression of chiP restores growth (Knopp and Andersson 2015).	Bacteria	Pseudomonadota	ChiP of E. coli (P75733)
1.B.25.1.14	OdpF (OccK2) glucuronate-selective porin; may also transport benzoate and vanillate (Eren et al., 2012). 3-d structure is known (3SZD).	Bacteria	Pseudomonadota	OdpF of Pseudomonas aeruginosa (Q9I6P8)
1.B.25.1.15	Outer membrane porin	Bacteria	Bacteroidota	Ftrac_3105 of Marivirga tractuosa
1.B.25.1.16	Outer membrane porin	Bacteria	Pseudomonadota	Tint_2055 of Thiomonas intermedia
1.B.25.1.17	Outer membrane porin	Bacteria	Campylobacterota	Sdel_0469 of Sulfurospirillum deleyianum
1.B.25.1.18	Outer membrane porin, OprD family	Bacteria	Aquificota	SULAZ_1441 of Sulfurihydrogenibium azorense
1.B.25.1.19	Outer membrane porin, OprD family	Bacteria	Pseudomonadota	PROVRUST_07396 of Providencia rustigianii DSM 4541
1.B.25.1.20	Outer membrane porin	Bacteria	Campylobacterota	Sulku_2564 of Sulfuricurvum kujiense
1.B.25.1.21	Outer membrane porin	Bacteria	Pseudomonadota	Atc_1106 of Acidithiobacillus caldus
1.B.25.1.22	Outer membrane porin	Bacteria	Campylobacterota	Sdel_0019 of Sulfurospirillum deleyianum
1.B.25.1.23	Outer membrane porin, OprD family	Bacteria	Pseudomonadota	Dsui_2952 of Azospira oryzae
1.B.25.1.24	Outer membrane porin, OprD family	Bacteria	Proteobacteria	CBGD1_2399 of Campylobacterales bacterium GD 1
1.B.25.1.25	Uncharacterized protein	Bacteria	Campylobacterota	SMGD1_0130 of Sulfurimonas gotlandica GD1
1.B.25.1.26	Outer membrane porin	Bacteria	Campylobacterota	Sulku_1154 of Sulfuricurvum kujiense
1.B.25.1.27	Outer membrane porin	Bacteria	Pseudomonadota	Sputcn32_0255 of Shewanella putrefaciens
1.B.25.1.28	Putative outer membrane porin	Bacteria	Campylobacterota	SMGD1_2744 of Sulfurimonas gotlandica GD1
1.B.25.1.29	Outer membrane porin	Bacteria	Campylobacterota	Sdel_2087 of Sulfurospirillum deleyianum
1.B.25.1.30	Outer membrane porin	Bacteria	Campylobacterota	Sulku_1034 of Sulfuricurvum kujiense
1.B.25.1.31	Putative porin	Bacteria	Pseudomonadota	Putative porin of Shewanella sediminis
1.B.25.1.32	Outer membrane tyrosine-specific porin, OpdT (Tamber et al. 2006).	Bacteria	Pseudomonadota	OpdT of Pseudomonas aeruginosa
1.B.25.1.33	Putative porin	Bacteria	Aquificota	Porin of Sulfurihydrogenibium azorense
1.B.25.1.34	The outer membrane porin, OdpQ of 421 aas. opdQ is transcriptionally repressed under low oxygen but increased in the presence of nitrate. The nitrate-induced regulation is dependent on NarL via the NarXL two-component system. In addition, NaCl-induced osmotic stress increases OpdQ production among most of the clinical strains evaluated (Fowler and Hanson 2015).	Bacteria	Pseudomonadota	OdpQ of Pseudomonas aeruginosa
1.B.25.1.35	Benzoate-specific porin protein of 397 aas and 1 N-terminal TMS, BenF (Choudhary et al. 2017).	Bacteria	Pseudomonadota	BenF of Pseudomonas putida
1.B.25.1.36	BenP porin (Clark et al. 2002). Probably transports aromatic compounds such as benzoate for degradation.	Bacteria	Pseudomonadota	BenP of Acinetobacter sp.ADP1 (Acinetobacter baylyi)
1.B.25.1.37	Putative porin of 430 aas and 1 N-terminal TMS, NicP.	Bacteria	Pseudomonadota	NicP of Pseudomonas putida
1.B.25.1.38	OprD or OccAB1 of 418 aas and 1 N-terminal TMS. The 3-d structure has been determined for 4 similar porins, OccAB1 - 4 (Zahn et al. 2016). Probably allows the uptake of small molecules including sugars, amino acids and some antibiotics. The transport properties have been studied (Benkerrou and Ceccarelli 2018).	Bacteria	Pseudomonadota	OprD of Acinetobacter baumannii
1.B.25.1.39	Outer membrane porin of 446 aas, OprE.	Bacteria	Pseudomonadota	OprE of Pseudomonas putida (Arthrobacter siderocapsulatus)
1.B.25.2.1	Putative porin of 278 aas	Bacteria	Lentisphaerota	PP of Lentisphaera araneosa
1.B.25.2.2	Uncharacterized outer membrane porin of 388 aas and 1 N-terminal TMS.	Bacteria	Campylobacterota	OMP of Sulfurospirillum barnesii
1.B.25.2.3	Putative porin of 402 aas.	Bacteria	Campylobacterota	Porin of Arcobacter porcinus]
1.B.25.3.1	Outer membrane porin, OprD, of 448 aas and 1 N-terminal TMS.	Bacteria	Pseudomonadota	OprD of Acinetobacter baumannii