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22  structures 1721  species 1  interaction 5579  sequences 106  architectures

Family: CHAP (PF05257)

Summary: CHAP domain

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CHAP domain Edit Wikipedia article

CHAP
PDB 2ioa EBI.jpg
E. coli Bifunctional glutathionylspermidine synthetase/amidase In complex with Mg2+ and ADP and phosphinate inhibitor.
Identifiers
Symbol CHAP
Pfam PF05257
Pfam clan CL0125
InterPro IPR007921
MEROPS C51

In molecular biology, the CHAP domain is a region between 110 and 140 amino acids that is found in proteins from bacteria, bacteriophages, archaea and eukaryotes of the Trypanosomidae family. The domain is named after the acronym cysteine, histidine-dependent amidohydrolases/peptidases. Many of these proteins are uncharacterised, but it has been proposed that they may function mainly in peptidoglycan hydrolysis. The CHAP domain is found in a wide range of protein architectures; it is commonly associated with bacterial type SH3 domains and with several families of amidase domains. It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack mechanism.[1][2]

The CHAP domain contains two invariant residues, a cysteine and a histidine. These residues form part of the putative active site of CHAP domain containing proteins. Secondary structure predictions show that the CHAP domain belongs to the alpha + beta structural class, with the N-terminal half largely containing predicted alpha helices and the C-terminal half principally composed of predicted beta strands.[1][2]

Some proteins known to contain a CHAP domain are listed below:

  • Bacterial and trypanosomal glutathionylspermidine amidases.
  • A variety of bacterial autolysins.
  • A Nocardia aerocolonigenes putative esterase.
  • Streptococcus pneumoniae choline-binding protein D.
  • Methanosarcina mazei protein MM2478, a putative chloride channel.
  • Several phage-encoded peptidoglycan hydrolases.
  • Cysteine peptidases belonging to MEROPS peptidase family C51 (D-alanyl-glycyl endopeptidase, clan CA).

References[edit]

  1. ^ a b Rigden DJ, Jedrzejas MJ, Galperin MY (May 2003). "Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases". Trends Biochem. Sci. 28 (5): 230–4. PMID 12765833. 
  2. ^ a b Bateman A, Rawlings ND (May 2003). "The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases". Trends Biochem. Sci. 28 (5): 234–7. doi:10.1016/S0968-0004(03)00061-6. PMID 12765834. 

This article incorporates text from the public domain Pfam and InterPro IPR007921

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

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CHAP domain Provide feedback

This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of P43675 where is functions as a glutathionylspermidine amidase EC:3.5.1.78 [1]. This domain is found to be the catalytic domain of PlyCA [4].

Literature references

  1. Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT; , J Biol Chem 1995;270:14031-14041.: Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. PUBMED:7775463 EPMC:7775463

  2. Bateman A, Rawlings ND; , Trends Biochem Sci 2003;28:234-237.: The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. PUBMED:12765834 EPMC:12765834

  3. Rigden DJ, Jedrzejas MJ, Galperin MY; , Trends Biochem Sci 2003;28:230-234.: Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases. PUBMED:12765833 EPMC:12765833

  4. Nelson D, Schuch R, Chahales P, Zhu S, Fischetti VA; , Proc Natl Acad Sci U S A. 2006;103:10765-10770.: PlyC: a multimeric bacteriophage lysin. PUBMED:16818874 EPMC:16818874


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007921

The CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain is a region between 110 and 140 amino acids that is found in proteins from bacteria, bacteriophages, archaea and eukaryotes of the Trypanosomidae family. Many of these proteins are uncharacterised, but it has been proposed that they may function mainly in peptidoglycan hydrolysis. The CHAP domain is found in a wide range of protein architectures; it is commonly associated with bacterial type SH3 domains and with several families of amidase domains. It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack mechanism [PUBMED:12765833, PUBMED:12765834].

The CHAP domain contains two invariant residues, a cysteine and a histidine. These residues form part of the putative active site of CHAP domain containing proteins. Secondary structure predictions show that the CHAP domain belongs to the alpha + beta structural class, with the N-terminal half largely containing predicted alpha helices and the C-terminal half principally composed of predicted beta strands [PUBMED:12765833, PUBMED:12765834].

Some proteins known to contain a CHAP domain are listed below:

  • Bacterial and trypanosomal glutathionylspermidine amidases.
  • A variety of bacterial autolysins.
  • A Nocardia aerocolonigenes putative esterase.
  • Streptococcus pneumoniae choline-binding protein D.
  • Methanosarcina mazei protein MM2478, a putative chloride channel.
  • Several phage-encoded peptidoglycan hydrolases.
  • Cysteine peptidases belonging to MEROPS peptidase family C51 (D-alanyl-glycyl endopeptidase, clan CA).

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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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.

  Seed
(47)
Full
(5579)
Representative proteomes NCBI
(2917)
Meta
(78)
RP15
(112)
RP35
(217)
RP55
(369)
RP75
(443)
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  Seed
(47)
Full
(5579)
Representative proteomes NCBI
(2917)
Meta
(78)
RP15
(112)
RP35
(217)
RP55
(369)
RP75
(443)
Alignment:
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Sequence:
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  Seed
(47)
Full
(5579)
Representative proteomes NCBI
(2917)
Meta
(78)
RP15
(112)
RP35
(217)
RP55
(369)
RP75
(443)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_2845 (release 7.7)
Previous IDs: AXE;
Type: Domain
Author: Bateman A
Number in seed: 47
Number in full: 5579
Average length of the domain: 122.10 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 30.57 %

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 25.2 25.2
Trusted cut-off 25.2 25.2
Noise cut-off 25.1 25.1
Model length: 125
Family (HMM) version: 11
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Species distribution

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Interactions

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

GSP_synth

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 CHAP domain has been found. There are 22 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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