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InterPro: IPR000064 NLP/P60

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UniProtKB

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4257 proteins

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Accession

IPR000064 NLP_P60

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00877	NLPC_P60	4257
Signatures in BioMart

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Found in

IPR011929 Putative phage cell wall peptidase, NlpC/P60

InterPro annotation

Entry Details in BioMart

Abstract

The Escherichia coli NLPC/Listeria P60 domain occurs at the C terminus of a number of different bacterial and viral proteins. The viral proteins are either described as tail assembly proteins or Gp19. In bacteria, the proteins are variously described as being putative tail component of prophage, invasin, invasion associated protein, putative lipoprotein, cell wall hydrolase, or putative endopeptidase.

The E. coli NLPC/Listeria P60 domain is contained within the boundaries of the cysteine peptidase domain that defines the MEROPS peptidase family C40 (clan C-). A type example being dipeptidyl-peptidase VI from Bacillus sphaericus and gamma-glutamyl-diamino acid-endopeptidase precursor from Lactococcus lactis EC:3.4.19.11. This group also contains proteins classified as non-peptidase homologues in that they either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases in the C40 family.

Structural links Help

PDB - click here

SCOP: d.3.1.16

Database links Help

PANDIT: PF00877

Blocks: IPB000064

MEROPS: C40

Pfam Clan: CL0125.11

Taxonomic coverage Help

Example proteins Help

P03729 Tail assembly protein K

P0AFV4 Lipoprotein spr

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000064	NLP/P60
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Help

Additional Reading Open in usermanual
	Anantharaman V, Aravind L. Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol. 4 2003 R11 [PubMed: 12620121] http://dx.doi.org/10.1186/gb-2003-4-2-r11
	Xu Q, Sudek S, McMullan D, Miller MD, Geierstanger B, Jones DH, Krishna SS, Spraggon G, Bursalay B, Abdubek P, Acosta C, Ambing E, Astakhova T, Axelrod HL, Carlton D, Caruthers J, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Won Han G, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Trout CV, van den Bedem H, Weekes D, White A, Wolf G, Zubieta C, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA. Structural basis of murein peptide specificity of a gamma-D-glutamyl-l-diamino acid endopeptidase. Structure 17 2009 303-13 [PubMed: 19217401] http://dx.doi.org/10.1016/j.str.2008.12.008

InterPro 23.1