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11  structures 1131  species 1  interaction 1227  sequences 4  architectures

Family: PLA1 (PF02253)

Summary: Phospholipase A1

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This is the Wikipedia entry entitled "Outer membrane phospholipase A1". More...

Outer membrane phospholipase A1 Edit Wikipedia article

Phospholipase A1
1qd6 opm.gif
Identifiers
Symbol PLA1
Pfam PF02253
InterPro IPR003187
SCOP 1qd6
SUPERFAMILY 1qd6
OPM superfamily 29
OPM protein 1qd6

Outer membrane phospholipase A1 (OMPLA) is an acyl hydrolase with a broad substrate specificity (EC:3.1.1.32.) from the bacterial outer membrane. It has been proposed that Ser164 is the active site of the protein (UniProt P00631) [1]

This integral membrane phospholipase was found in many Gram-negative bacteria and has a broad substrate specificity EC 3.1.1.32. The role of OMPLA has been most thoroughly studied in Escherichia coli, where it participates in the secretion of bacteriocins. Bacteriocin release is triggered by a lysis protein (bacteriocin release protein or BRP), followed by a phospholipase dependent accumulation of lysophospholipids and free fatty acids in the outer membrane.[2] The reaction products enhance the permeability of the outer membrane, which allows the semispecific secretion of bacteriocins. One speculative function of OMPLA is related to organic solvent tolerance in bacteria.

Structurally, it consists of a 12-stranded antiparallel beta-barrel with a convex and a flat side. The active site residues are exposed on the exterior of the flat face of the beta-barrel. The activity of the enzyme is regulated by reversible dimerisation. Dimer interactions occur exclusively in the membrane-embedded parts of the flat side of the beta-barrel, with polar residues embedded in an apolar environment forming the key interactions. The active site His and Ser residues are located at the exterior of the beta-barrel, at the outer leaflet side of the membrane. This location indicates that under normal conditions the substrate and the active site are physically separated, since in E. coli phospholipids are exclusively located in the inner leaflet of the outer membrane.[3]

References[edit]

  1. ^ Horrevoets, A. J.; Verheij, H. M.; De Haas, G. H. (1991). "Inactivation of Escherichia coli outer-membrane phospholipase a by the affinity label hexadecanesulfonyl fluoride. Evidence for an active-site serine". European journal of biochemistry / FEBS 198 (1): 247–253. PMID 2040286. 
  2. ^ Snijder, H. J.; Timmins, P. A.; Kalk, K. H.; Dijkstra, B. W. (2003). "Detergent organisation in crystals of monomeric outer membrane phospholipase A". Journal of structural biology 141 (2): 122–131. doi:10.1016/S1047-8477(02)00579-8. PMID 12615538. 
  3. ^ IPR003187


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Phospholipase A1 Provide feedback

Phospholipase A1 is a bacterial outer membrane bound acyl hydrolase with a broad substrate specificity EC:3.1.1.32. It has been proposed that Ser164 is the active site for P00631 [1].

Literature references

  1. Horrevoets AJ, Verheij HM, de Haas GH; , Eur J Biochem 1991;198:247-253.: Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active-site serine. PUBMED:2040286 EPMC:2040286


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003187

Outer membrane phospholipase A (OMPLA) is an integral membrane phospholipase, which is present in many Gram-negative bacteria and has a broad substrate specificity EC. The role of OMPLA has been most thoroughly studied in Escherichia coli, where it participates in the secretion of bacteriocins. Bacteriocin release is triggered by a lysis protein (bacteriocin release protein or BRP), followed by a phospholipase dependent accumulation of lysophospholipids and free fatty acids in the outer membrane [PUBMED:12615538]. The reaction products enhance the permeability of the outer membrane, which allows the semispecific secretion of bacteriocins. One speculative function of OMPLA is related to organic solvent tolerance in bacteria.

Structurally, it consists of a 12-stranded antiparallel beta-barrel with a convex and a flat side. The active site residues are exposed on the exterior of the flat face of the beta-barrel. The activity of the enzyme is regulated by reversible dimerisation. Dimer interactions occur exclusively in the membrane-embedded parts of the flat side of the beta-barrel, with polar residues embedded in an apolar environment forming the key interactions. The active site His and Ser residues are located at the exterior of the beta-barrel, at the outer leaflet side of the membrane. This location indicates that under normal conditions the substrate and the active site are physically separated, since in E. coli phospholipids are exclusively located in the inner leaflet of the outer membrane.

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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(78)
Full
(1227)
Representative proteomes NCBI
(747)
Meta
(50)
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(39)
RP35
(107)
RP55
(161)
RP75
(196)
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  Seed
(78)
Full
(1227)
Representative proteomes NCBI
(747)
Meta
(50)
RP15
(39)
RP35
(107)
RP55
(161)
RP75
(196)
Alignment:
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  Seed
(78)
Full
(1227)
Representative proteomes NCBI
(747)
Meta
(50)
RP15
(39)
RP35
(107)
RP55
(161)
RP75
(196)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_3500 (release 5.2)
Previous IDs: none
Type: Domain
Author: Bateman A, Mian N
Number in seed: 78
Number in full: 1227
Average length of the domain: 244.60 aa
Average identity of full alignment: 43 %
Average coverage of the sequence by the domain: 80.00 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.7 19.7
Trusted cut-off 19.8 22.8
Noise cut-off 18.3 19.0
Model length: 260
Family (HMM) version: 10
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Species distribution

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Interactions

There is 1 interaction for this family. More...

PLA1

Structures

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 PLA1 domain has been found. There are 11 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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