LCP family explained

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,), 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,)^[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]

External links

• MetaCyc RXN-18030: Polyisoprenyl-teichoic acid—peptidoglycan teichoic acid transferase

Notes and References

1. Lazarevic V, Margot P, Soldo B, Karamata D . Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier . Journal of General Microbiology . 138 . 9 . 1949–61 . September 1992 . 1357079 . 10.1099/00221287-138-9-1949 . free .
2. Kawai Y, Marles-Wright J, Cleverley RM, Emmins R, Ishikawa S, Kuwano M, Heinz N, Bui NK, Hoyland CN, Ogasawara N, Lewis RJ, Vollmer W, Daniel RA, Errington J . 6 . A widespread family of bacterial cell wall assembly proteins . The EMBO Journal . 30 . 24 . 4931–41 . September 2011 . 21964069 . 3243631 . 10.1038/emboj.2011.358 .
3. Wang Q, Zhu L, Jones V, Wang C, Hua Y, Shi X, Feng X, Jackson M, Niu C, Gao Q . 6 . 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 . July 2015 . 25939506 . 10.1128/IAI.03081-14 . 4468561 . free .
4. Maréchal M, Amoroso A, Morlot C, Vernet T, Coyette J, Joris B . Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site . BMC Microbiology . 16 . 1 . 239 . October 2016 . 27729019 . 10.1186/s12866-016-0844-y . 5059904 . free .
5. Amer BR, Clubb RT . A sweet new role for LCP enzymes in protein glycosylation . Molecular Microbiology . 94 . 6 . 1197–200 . December 2014 . 25302626 . 10.1111/mmi.12825 . 4262582 . free .
6. Percy MG, Gründling A . Lipoteichoic acid synthesis and function in gram-positive bacteria . Annual Review of Microbiology . 68 . 1 . 81–100 . 8 September 2014 . 24819367 . 10.1146/annurev-micro-091213-112949 . free .
7. Siegel SD, Amer BR, Wu C, Sawaya MR, Gosschalk JE, Clubb RT, Ton-That H . Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein . mBio . 10 . 1 . February 2019 . 30782654 . 6381275 . 10.1128/mBio.01580-18 . free .