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InterPro: IPR002482 Peptidoglycan-binding Lysin subgroup

Protein matchesHelp
UniProtKB
Matches:
7319 proteins
AccessionHelp IPR002482 Peptidoglycan-bd_Lysin_sg
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR018392 Peptidoglycan-binding lysin domain
Children IPR014248 Spore coat assembly protein SafA
Found in IPR014256 Sporulation stage VI, protein D
GO Term annotationHelp
Process GO:0016998 cell wall macromolecule catabolic process
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is about 40 residues long and is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function.

Structural linksHelp
SCOP: d.7.1.1
CATH: 3.10.350.10
Database linksHelp
PANDIT: PF01476
Blocks: IPB002482

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002482 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O05495 Putative sporulation-specific glycosylase ydhD

O23006 LysM domain-containing GPI-anchored protein 2

Q4KMM3 Oxidation resistance protein 1

Q8H8C7 Chitin elicitor-binding protein

Q96S90 LysM and putative peptidoglycan-binding domain-containing protein 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR002482 Peptidoglycan-binding Lysin subgroup
IPR018392 Peptidoglycan-binding lysin domain
IPR017853 Glycoside hydrolase, catalytic core
IPR011583 Chitinase II
IPR004182 GRAM
IPR006571 TLDc
IPR001223 Glycoside hydrolase, family 18, catalytic domain
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L, Shockman GD, Ghuysen JM.
Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin.
FEMS Microbiol. Lett. 70 257-64 1992 [PubMed: 1352512]
http://dx.doi.org/10.1016/0378-1097(92)90707-U

Additional ReadingHelp
Bateman A, Bycroft M.
The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD).
J. Mol. Biol. 299 2000 1113-9 [PubMed: 10843862]
http://dx.doi.org/10.1006/jmbi.2000.3778
Birkeland NK.
Cloning, molecular characterization, and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: a dual lysis system of modular design.
Can. J. Microbiol. 40 1994 658-65 [PubMed: 7922887]
Bielnicki J, Devedjiev Y, Derewenda U, Dauter Z, Joachimiak A, Derewenda ZS.
B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes.
Proteins 62 2006 144-51 [PubMed: 16287140]
http://dx.doi.org/10.1002/prot.20702
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InterPro 23.1