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Links from Protein

Items: 9

1.

Csd3 second domain

This entry represents the second domain from the Csd3 peptidase [2]. This domain has a similar structure to Pfam:PF18059 despite low sequence similarity [2]. Paper describing PDB structure 2gu1. [1]. 18498110. Crystal structure of a putative lysostaphin peptidase from. Vibrio cholerae.. Ragumani S, Kumaran D, Burley SK, Swaminathan S;. Proteins. 2008;72:1096-1103.. Paper describing PDB structure 4rny. [2]. 25760614. Structure of Csd3 from Helicobacter pylori, a cell. shape-determining metallopeptidase.. An DR, Kim HS, Kim J, Im HN, Yoon HJ, Yoon JY, Jang JY, Hesek D,. Lee M, Mobashery S, Kim SJ, Lee BI, Suh SW;. Acta Crystallogr D Biol Crystallogr. 2015;71:675-686. (from Pfam)

Date:
2024-08-14
Family Accession:
NF039309.4
Method:
HMM
2.

LysM-like peptidoglycan-binding domain-containing protein

The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A [1]. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation [1]. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB [3]. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments [3]. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links [4]. The OapA domain is distantly related to Pfam:PF01476. [1]. 8559074. Identification and characterization of a cell envelope protein. of Haemophilus influenzae contributing to phase variation in. colony opacity and nasopharyngeal colonization.. Weiser JN, Chong ST, Greenberg D, Fong W;. Mol Microbiol 1995;17:555-564.. [2]. 8830271. Phenotypic switching of Haemophilus influenzae.. Moxon ER, Gewurz BE, Richards JC, Inzana T, Jennings MP, Hood. DW;. Mol Microbiol 1996;19:1149-1150.. [3]. 23565292. Harnessing single cell sorting to identify cell division genes. and regulators in bacteria.. Burke C, Liu M, Britton W, Triccas JA, Thomas T, Smith AL, Allen. S, Salomon R, Harry E;. PLoS One. 2013;8:e60964.. [4]. 29686141. YtfB, an OapA Domain-Containing Protein, Is a New Cell Division. Protein in Escherichia coli.. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Molecular Function:
peptidoglycan binding (GO:0042834)
Date:
2024-08-14
Family Accession:
NF016140.5
Method:
HMM
3.

peptidoglycan DD-metalloendopeptidase family protein

Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown. (from Pfam)

Date:
2024-08-14
Family Accession:
NF013700.5
Method:
HMM
4.
new record, indexing in progress
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5.
new record, indexing in progress
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new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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