The LCP family or TagU family of proteins is a conserved family of phosphotransferases that are involved in the attachment of teichoic acid (TA) molecules to gram-positive cell wall or cell membrane. It was initially thought as the LytR (lytic repressor) component of a LytABC operon encoding autolysins,[1] but the mechanism of regulation was later realized to be the production of TA molecules. It was accordingly renamed TagU.[2]
The "LCP" acronym derives from three proteins initially identified to contain this domain, LytR (now TagU, Q02115), cpsA ("Capsular polysaccharide expression regulator"), and psr ("PBP 5 synthesis repressor"). These proteins were mistaken as transcriptional regulators via different reasons, but all three of them are now known to be TagU-like enzymes.[3][4] While TagU itself only attaches TA molecules to the peptidoglycan cell wall (forming WTA), other LCP proteins may glycosylate cell wall proteins (A. oris LcpA, PDB: 5V8C)[5] or attach TA molecules to a cell membrane anchor (forming LTA).[6] Most, if not all, LCP proteins also have a secondary pyrophosphatase activity.[7]
Typical TagU proteins are made up of an N-terminal transmembrane domain (for anchoring), an optional, non-conserved accessory domain (CATH 3tflA01), a core catalytic domain, and sometimes a C-terminal domain for which the structure is unknown. The core LCP domain is a magnesium-dependent enzyme.[2]
^ abKawai Y, Marles-Wright J, Cleverley RM, Emmins R, Ishikawa S, Kuwano M, et al. (September 2011). "A widespread family of bacterial cell wall assembly proteins". The EMBO Journal. 30 (24): 4931–41. doi:10.1038/emboj.2011.358. PMC3243631. PMID21964069.4931-41&rft.date=2011-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243631#id-name=PMC&rft_id=info:pmid/21964069&rft_id=info:doi/10.1038/emboj.2011.358&rft.aulast=Kawai&rft.aufirst=Y&rft.au=Marles-Wright, J&rft.au=Cleverley, RM&rft.au=Emmins, R&rft.au=Ishikawa, S&rft.au=Kuwano, M&rft.au=Heinz, N&rft.au=Bui, NK&rft.au=Hoyland, CN&rft.au=Ogasawara, N&rft.au=Lewis, RJ&rft.au=Vollmer, W&rft.au=Daniel, RA&rft.au=Errington, J&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243631&rfr_id=info:sid/en.wikipedia.org:LCP family" class="Z3988">
^Wang Q, Zhu L, Jones V, Wang C, Hua Y, Shi X, et al. (July 2015). "CpsA, a LytR-CpsA-Psr Family Protein in Mycobacterium marinum, Is Required for Cell Wall Integrity and Virulence". Infection and Immunity. 83 (7): 2844–54. doi:10.1128/IAI.03081-14. PMC4468561. PMID25939506.2844-54&rft.date=2015-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468561#id-name=PMC&rft_id=info:pmid/25939506&rft_id=info:doi/10.1128/IAI.03081-14&rft.aulast=Wang&rft.aufirst=Q&rft.au=Zhu, L&rft.au=Jones, V&rft.au=Wang, C&rft.au=Hua, Y&rft.au=Shi, X&rft.au=Feng, X&rft.au=Jackson, M&rft.au=Niu, C&rft.au=Gao, Q&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468561&rfr_id=info:sid/en.wikipedia.org:LCP family" class="Z3988">
^Amer BR, Clubb RT (December 2014). "A sweet new role for LCP enzymes in protein glycosylation". Molecular Microbiology. 94 (6): 1197–200. doi:10.1111/mmi.12825. PMC4262582. PMID25302626.1197-200&rft.date=2014-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4262582#id-name=PMC&rft_id=info:pmid/25302626&rft_id=info:doi/10.1111/mmi.12825&rft.aulast=Amer&rft.aufirst=BR&rft.au=Clubb, RT&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4262582&rfr_id=info:sid/en.wikipedia.org:LCP family" class="Z3988">
^Percy MG, Gründling A (8 September 2014). "Lipoteichoic acid synthesis and function in gram-positive bacteria". Annual Review of Microbiology. 68 (1): 81–100. doi:10.1146/annurev-micro-091213-112949. PMID24819367.81-100&rft.date=2014-09-08&rft_id=info:doi/10.1146/annurev-micro-091213-112949&rft_id=info:pmid/24819367&rft.aulast=Percy&rft.aufirst=MG&rft.au=Gründling, A&rft_id=https://doi.org/10.1146%2Fannurev-micro-091213-112949&rfr_id=info:sid/en.wikipedia.org:LCP family" class="Z3988">
