describes same family; this is the full-length protein
LytR/CpsA/Psr, C-terminal domain
Identifiers
Symbol
LytR_C
Pfam
PF13399
InterPro
IPR027381
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
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]
^Lazarevic V, Margot P, Soldo B, Karamata D (September 1992). "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. doi:10.1099/00221287-138-9-1949. PMID 1357079.
^ 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. PMC 3243631. PMID 21964069.
^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. PMC 4468561. PMID 25939506.
^Maréchal M, Amoroso A, Morlot C, Vernet T, Coyette J, Joris B (October 2016). "Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site". BMC Microbiology. 16 (1): 239. doi:10.1186/s12866-016-0844-y. PMC 5059904. PMID 27729019.
^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. PMC 4262582. PMID 25302626.
^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. PMID 24819367.
^Siegel SD, Amer BR, Wu C, Sawaya MR, Gosschalk JE, Clubb RT, Ton-That H (February 2019). "Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein". mBio. 10 (1). doi:10.1128/mBio.01580-18. PMC 6381275. PMID 30782654.
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