{"doi":"10.1111/1462-2920.15038","title":"<scp>PapA</scp>\n                    , a peptidoglycan‐associated protein, interacts with\n                    <scp>OmpC</scp>\n                    and maintains cell envelope integrity","abstract":"<jats:title>Summary</jats:title>\n                  <jats:p>\n                    The bacterial cell envelope is critical to support and maintain cellular life. In Gram‐negative bacterial cells, the outer membrane and the peptidoglycan layer are two important parts of the cell envelope and they harbour abundant proteins. Here, we report the identification and characterization of a previously unknown\n                    <jats:styled-content>p</jats:styled-content>\n                    eptidoglycan‐\n                    <jats:styled-content>a</jats:styled-content>\n                    ssociated\n                    <jats:styled-content>p</jats:styled-content>\n                    rotein, PapA, from the Gram‐negative\n                    <jats:italic>Comamonas testosteroni</jats:italic>\n                    . PapA bound peptidoglycan with its C‐terminal domain and interacted with the outer‐membrane porin OmpC. The PapA‐OmpC complex riveted the outer membrane and the peptidoglycan layer, and played a role in maintaining cell envelope integrity. When\n                    <jats:italic>papA</jats:italic>\n                    was disrupted, the mutant CNB‐1Δ\n                    <jats:italic>papA</jats:italic>\n                    apparently had an outer membrane partly separated from the peptidoglycan layer. Phenotypically, the mutant CNB‐1Δ\n                    <jats:italic>papA</jats:italic>\n                    lost chemotactic responses and had longer lag‐phase of growth, less flagellation and higher sensitivity to harsh environments. Totally, 1093 functionally unknown PapA homologues were identified from the public NR protein database and they were mainly distributed in Burkholderiales of Betaproteobacteria. Our finding provides a clue that the PapA homologous proteins might function as a rivet to maintain cell envelope integrity in those Gram‐negative bacteria.\n                  </jats:p>","journal":"Environmental Microbiology","year":2021,"id":596785,"datarank":0.26876392038420827,"base_score":1.791759469228055,"endowment":1.791759469228055,"self_citation_contribution":0.26876392038420827,"citation_network_contribution":0.0,"self_endowment_contribution":0.26876392038420827,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":5,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1528559,"name":"Hong‐He Chen","orcid":null,"position":1,"is_corresponding":false},{"id":821389,"name":"Zhou Huang","orcid":"0000-0003-1850-5296","position":2,"is_corresponding":false},{"id":1528560,"name":"Xiao‐Jing Li","orcid":null,"position":3,"is_corresponding":false},{"id":1377373,"name":"Nan Zhou","orcid":"0000-0001-5549-1335","position":4,"is_corresponding":false},{"id":972024,"name":"Chang Liu","orcid":"0000-0001-7951-4546","position":5,"is_corresponding":false},{"id":1094950,"name":"Cheng‐Ying Jiang","orcid":"0000-0003-0257-0982","position":6,"is_corresponding":false},{"id":1094951,"name":"De‐Feng Li","orcid":"0000-0002-8683-019X","position":7,"is_corresponding":false},{"id":4808,"name":"Shuang‐Jiang Liu","orcid":"0000-0002-7585-310X","position":8,"is_corresponding":false},{"id":1094947,"name":"Yun‐Hao Wang","orcid":"0000-0001-9934-3852","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"<scp>PapA</scp>\n                    , a peptidoglycan‐associated protein, interacts with\n                    <scp>OmpC</scp>\n                    and maintains cell envelope integrity","abstract":"<jats:title>Summary</jats:title>\n                  <jats:p>\n                    The bacterial cell envelope is critical to support and maintain cellular life. In Gram‐negative bacterial cells, the outer membrane and the peptidoglycan layer are two important parts of the cell envelope and they harbour abundant proteins. Here, we report the identification and characterization of a previously unknown\n                    <jats:styled-content>p</jats:styled-content>\n                    eptidoglycan‐\n                    <jats:styled-content>a</jats:styled-content>\n                    ssociated\n                    <jats:styled-content>p</jats:styled-content>\n                    rotein, PapA, from the Gram‐negative\n                    <jats:italic>Comamonas testosteroni</jats:italic>\n                    . PapA bound peptidoglycan with its C‐terminal domain and interacted with the outer‐membrane porin OmpC. The PapA‐OmpC complex riveted the outer membrane and the peptidoglycan layer, and played a role in maintaining cell envelope integrity. When\n                    <jats:italic>papA</jats:italic>\n                    was disrupted, the mutant CNB‐1Δ\n                    <jats:italic>papA</jats:italic>\n                    apparently had an outer membrane partly separated from the peptidoglycan layer. Phenotypically, the mutant CNB‐1Δ\n                    <jats:italic>papA</jats:italic>\n                    lost chemotactic responses and had longer lag‐phase of growth, less flagellation and higher sensitivity to harsh environments. Totally, 1093 functionally unknown PapA homologues were identified from the public NR protein database and they were mainly distributed in Burkholderiales of Betaproteobacteria. Our finding provides a clue that the PapA homologous proteins might function as a rivet to maintain cell envelope integrity in those Gram‐negative bacteria.\n                  </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"32329167","pmcid":null,"openalex_id":"https://openalex.org/W32329167","authors":[],"funders":[{"funder_name":"National Natural Science Foundation of China","grant_id":"31861133002","title":null},{"funder_name":"National Key R&amp;D Program of China","grant_id":"2019YFA0905500","title":null}],"total_grants":2,"fwci":0.0,"citation_percentile":0.00973361,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2F1462-2920.15038","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1111/1462-2920.15038","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/full-xml/10.1111/1462-2920.15038","host_type":"publisher"},{"url":"https://sfamjournals.onlinelibrary.wiley.com/doi/pdf/10.1111/1462-2920.15038","host_type":"publisher"},{"url":"https://dialnet.unirioja.es/servlet/articulo?codigo=101554","host_type":"journal"}],"fields_of_study":["Galician and Iberian cultural studies","Bacterial Outer Membrane Proteins","Cell Membrane","Cell Wall","Gram-Negative Bacteria","Peptidoglycan","Porins","Protein Binding"],"mesh_terms":["Cell Membrane","Cell Wall","Gram-Negative Bacteria","Peptidoglycan","Bacterial Outer Membrane Proteins","Porins","Protein Binding"],"keywords":["Geography"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-28T11:15:30.196151Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}