Editing Transmembrane protein (section)

==3D structures==
{{see also|Transporter Classification Database}}

===Light absorption-driven transporters===
* [[Bacteriorhodopsin]]-like proteins including [[rhodopsin]] (see also [[opsin]])
* Bacterial [[photosynthetic reaction centre]]s and [[photosystem]]s I and II
* [[Light-harvesting complex]]es from [[bacteria]] and [[chloroplasts]]

===Oxidoreduction-driven transporters===
* Transmembrane cytochrome b-like proteins: [[coenzyme Q - cytochrome c reductase]] (cytochrome bc1 ); [[cytochrome b6f complex]]; formate dehydrogenase, respiratory [[nitrate reductase]]; [[succinate - coenzyme Q reductase]] (fumarate reductase); and [[succinate dehydrogenase]]. See [[electron transport chain]].
* [[Cytochrome c oxidase]]s from [[bacteria]] and [[mitochondria]]

===Electrochemical potential-driven transporters===
* Proton or sodium translocating F-type and V-type [[ATPase]]s

===P-P-bond hydrolysis-driven transporters===
* P-type [[calcium ATPase]] (five different conformations)
* Calcium ATPase regulators [[phospholamban]] and [[sarcolipin]]
* [[ABC transporter]]s
* General [[secretory pathway]] (Sec) [[translocon]] (preprotein translocase SecY)

===Porters (uniporters, symporters, antiporters)===
* [[Mitochondrial]] [[carrier protein]]s
* Major Facilitator Superfamily (Glycerol-3-phosphate transporter, Lactose [[permease]], and Multidrug transporter EmrD)
* [[Resistance-Nodulation-Cell Division Superfamily (RND)|Resistance-nodulation-cell division]] (multidrug [[efflux (microbiology)|efflux]] transporter AcrB, see [[multidrug resistance]])
* Dicarboxylate/amino acid:cation symporter (proton glutamate symporter)
* Monovalent cation/proton antiporter (Sodium/proton antiporter 1 NhaA)
* [[Neurotransmitter]] sodium symporter
* Ammonia transporters
* Drug/Metabolite Transporter (small multidrug resistance transporter EmrE - the structures are retracted as erroneous)

===Alpha-helical channels including ion channels===
* [[Voltage-gated ion channel]] like, including [[potassium channel]]s KcsA and KvAP, and [[inward-rectifier potassium ion channel]] Kirbac
* [[Large-conductance mechanosensitive channel, MscL]]
* [[Mechanosensitive ion channel|Small-conductance mechanosensitive ion channel (MscS)]]
* [[Magnesium transporters|CorA metal ion transporters]]
* [[Ligand-gated ion channel]] of [[neurotransmitter]] receptors ([[acetylcholine receptor]])
* [[Aquaporin]]s
* [[Chloride channel]]s
* Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane proteins from the outer bacterial membrane

===Enzymes===
* [[Methane monooxygenase]]
* [[Rhomboid protease]]
* [[Disulfide bond]] formation protein (DsbA-DsbB complex)

===Proteins with single transmembrane alpha-helices===
* Subunits of [[T cell receptor]] complex 
* Cytochrome c [[nitrite reductase]] complex
* [[Glycophorin]] A dimer
* Inovirus ([[filamentous phage]]) major coat protein
* [[Pilin]]
* [[Pulmonary surfactant]]-associated protein
* [[Monoamine oxidase]]s A and B
* [[Fatty acid amide hydrolase]]<ref name="pmid12459591">{{cite journal |vauthors=Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF | s2cid = 22656813 | title = Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling | journal = Science | volume = 298 | issue = 5599 | pages = 1793–6 |date=November 2002 | pmid = 12459591 | doi = 10.1126/science.1076535 | bibcode = 2002Sci...298.1793B }}</ref>
* [[Cytochrome P450 oxidase]]s
* [[Mineralocorticoid|Corticosteroid 11β-dehydrogenases]] .
* [[Signal Peptide Peptidase]]

===Beta-barrels composed of a single polypeptide chain===
* Beta barrels from eight beta-strands and with "shear number" of ten (''n=8, S=10''). They include:
** [[OmpA-like transmembrane domain]] (OmpA)
** [[Virulence-related outer membrane protein family]] (OmpX)
** [[Outer membrane protein W family]] (OmpW)
** [[Antimicrobial peptide resistance and lipid A acylation protein family]] (PagP)
** [[Lipid A deacylase PagL]]
** [[Opacity family porins]] (NspA)
* [[Autotransporter domain]] (''n=12,S=14'')
* [[FadL outer membrane protein transport family]], including [[Fatty acid]] transporter FadL (''n=14,S=14'')
* [[General bacterial porin family]], known as trimeric [[porin (protein)|porins]] (''n=16,S=20'')
* [[Maltoporin]], or sugar [[porin (protein)|porins]] (''n=18,S=22'')
* [[Nucleoside-specific porin]] (''n=12,S=16'')
* [[Outer membrane phospholipase A1]](''n=12,S=16'')
* [[TonB-dependent receptors]] and their [[TonB-dependent receptors#Plug domain|plug domain]]. They are ligand-gated outer membrane channels (''n=22,S=24''), including [[cobalamin]] transporter BtuB, Fe(III)-pyochelin receptor FptA, receptor FepA, ferric hydroxamate uptake receptor FhuA, transporter FecA, and pyoverdine receptor FpvA
* [[Outer membrane protein OpcA]] family (''n=10,S=12'') that includes outer membrane [[protease]] OmpT and [[Outer membrane protein OpcA|adhesin/invasin OpcA protein]]
* [[Outer membrane protein G]] porin family (''n=14,S=16'')

Note: ''n'' and ''S'' are, respectively, the number of beta-strands and the "shear number"<ref>{{cite journal |doi=10.1016/0022-2836(94)90064-7 |vauthors=Murzin AG, Lesk AM, Chothia C |title=Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis |journal=J. Mol. Biol. |volume=236 |issue=5 |pages=1369–81 |date=March 1994 |pmid=8126726 }}</ref> of the [[beta-barrel]]

===Beta-barrels composed of several polypeptide chains===
* [[Trimeric Autotransporter Adhesins (TAA)|Trimeric autotransporter]] (''n=12,S=12'')
* [[Outer membrane efflux proteins]], also known as trimeric outer membrane factors (n=12,S=18) including TolC and multidrug resistance proteins
* [[MspA porin]] (octamer, ''n=S=16'') and α-hemolysin (heptamer ''n=S=14'') . These proteins are secreted.