Summary: Outer membrane protein transport protein (OMPP1/FadL/TodX)
This is the Wikipedia entry entitled "FadL outer membrane protein transport family". More...
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FadL outer membrane protein transport family Edit Wikipedia article
|Outer membrane transport proteins (OMPP1/FadL/TodX)|
Structure of the bacterial fatty acid transporter FadL.
Outer membrane transport proteins (OMPP1/FadL/TodX) family includes several proteins that are involved in toluene catabolism and degradation of aromatic hydrocarbons. This family also includes protein FadL involved in translocation of long-chain fatty acids across the outer membrane. It is also a receptor for the bacteriophage T2.
- Wang, Y.; Rawlings, M.; Gibson, D. T.; Labbé, D.; Bergeron, H.; Brousseau, R.; Lau, P. C. (1995). "Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1". Molecular & general genetics : MGG 246 (5): 570–579. doi:10.1007/bf00298963. PMID 7535376.
- Kahng, H. Y.; Byrne, A. M.; Olsen, R. H.; Kukor, J. J. (2000). "Characterization and role of tbuX in utilization of toluene by Ralstonia pickettii PKO1". Journal of Bacteriology 182 (5): 1232–1242. doi:10.1128/jb.182.5.1232-1242.2000. PMC 94407. PMID 10671442.
- Eaton, R. W. (1997). "P-Cymene catabolic pathway in Pseudomonas putida F1: Cloning and characterization of DNA encoding conversion of p-cymene to p-cumate". Journal of Bacteriology 179 (10): 3171–3180. PMC 179094. PMID 9150211.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Outer membrane protein transport protein (OMPP1/FadL/TodX) Provide feedback
This family includes TodX from Pseudomonas putida F1 Q51971 and TbuX from Ralstonia pickettii PKO1 Q9RBW8. These are membrane proteins of uncertain function that are involved in toluene catabolism. Related proteins involved in the degradation of similar aromatic hydrocarbons are also in this family, such as CymD O33458. This family also includes FadL involved in translocation of long-chain fatty acids across the outer membrane. It is also a receptor for the bacteriophage T2.
Wang Y, Rawlings M, Gibson DT, Labbe D, Bergeron H, Brousseau R, Lau PC; , Mol Gen Genet 1995;246:570-579.: Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1. PUBMED:7535376 EPMC:7535376
Eaton RW; , J Bacteriol 1997;179:3171-3180.: p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate. PUBMED:9150211 EPMC:9150211
Internal database links
|SCOOP:||UPF0164 Autotransporter YadA_anchor BBP2 DUF2490 DUF3308 MtrB_PioB OMP_b-brl OMP_b-brl_2 Porin_4|
|Similarity to PfamA using HHSearch:||DUF2490|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005017
This family includes TodX from Pseudomonas putida (strain F1/ATCC 700007) SWISSPROT and TbuX from Burkholderia pickettii (Ralstonia pickettii) (Pseudomonas pickettii) PKO1 SWISSPROT. These are membrane proteins of uncertain function that are involved in toluene catabolism. Related proteins involved in the degradation of similar aromatic hydrocarbons are also in this family, such as CymD SWISSPROT.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
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This clan gathers together a large set of beta barrel membrane proteins.Although these proteins have different numbers of beta strands in the barrel they have significant sequence similarity between families.
The clan contains the following 63 members:Ail_Lom Autotransporter Bac_surface_Ag BBP2 BBP2_2 Campylo_MOMP Channel_Tsx CopB DUF2490 DUF2860 DUF3078 DUF3138 DUF3187 DUF3308 DUF3575 DUF481 DUF560 Gcw_chp HP_OMP HP_OMP_2 KdgM LamB Legionella_OMP Lipoprot_C MDM10 MipA MSP MtrB_PioB Omp_AT OMP_b-brl OMP_b-brl_2 OMP_b-brl_3 OmpA_like OmpA_membrane Omptin OmpW Opacity OpcA OprB OprD OprF OstA_C PagL PagP Phenol_MetA_deg Porin_1 Porin_10 Porin_2 Porin_3 Porin_4 Porin_7 Porin_8 Porin_O_P Porin_OmpG ShlB Surface_Ag_2 TcfC Toluene_X TonB_dep_Rec TraF_2 TSA Usher YfaZ
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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Curation and family details
|Seed source:||Pfam-B_3708 (release 6.5)|
|Number in seed:||12|
|Number in full:||753|
|Average length of the domain:||380.10 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||89.00 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toluene_X domain has been found. There are 33 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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