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InterPro: IPR001279 Beta-lactamase-like

Protein matches Help

UniProtKB

Matches:

19429 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001279 Blactmase-like

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SMART	SM00849	Lactamase_B	19429
Signatures in BioMart

InterPro Relationships Help

Children

IPR013470 Ribonuclease Z, Thermotoga maritima
IPR013471 Ribonuclease Z
IPR017693 Phosphonate metabolism protein PhnP
IPR017782 Hydroxyacylglutathione hydrolase

Found in

IPR004613 Ribonuclease J
IPR004797 Competence protein ComEC/Rec2
IPR014426 Uncharacterised conserved protein UCP004944, hydrolase, metallo-beta-lactamase
IPR016440 Rubredoxin-oxygen oxidoreductase
IPR019975 KH-domain/beta-lactamase-domain protein, archaea

Contains

IPR001018 Beta-lactamase, class B, conserved site

GO Term annotation Help

Function

GO:0016787 hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

Apart from the beta-lactamases a number of other proteins contain this domain [1]. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.

Structural links Help

PDB - click here

SCOP: d.157.1.1 , d.157.1.10 , d.157.1.11 , d.157.1.12 , d.157.1.13 , d.157.1.14 , d.157.1.2 , d.157.1.3 , d.157.1.5 , d.157.1.7 , d.157.1.8 , d.157.1.9

CATH: 3.60.15.10

Database links Help

PANDIT: PF00753

Blocks: IPB001279

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001279

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O17403 Probable cleavage and polyadenylation specificity factor subunit 2

O35218 Cleavage and polyadenylation specificity factor subunit 2

Q05584 Hydroxyacylglutathione hydrolase, cytoplasmic isozyme

Q16775 Hydroxyacylglutathione hydrolase, mitochondrial

Q8MKW7 Ribonuclease Z, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011108	RNA-metabolising metallo-beta-lactamase
IPR017782	Hydroxyacylglutathione hydrolase
IPR001279	Beta-lactamase-like
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 4914-21 1995 [PubMed: 7588620] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7588620

Additional Reading Open in usermanual
	Di Matteo A, Scandurra FM, Testa F, Forte E, Sarti P, Brunori M, Giuffre A. The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalis. J. Biol. Chem. 283 2008 4061-8 [PubMed: 18077462] http://dx.doi.org/10.1074/jbc.M705605200
	Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O. The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J. Mol. Biol. 375 2008 604-11 [PubMed: 18061205] http://dx.doi.org/10.1016/j.jmb.2007.11.012
	Lienard BM, Garau G, Horsfall L, Karsisiotis AI, Damblon C, Lassaux P, Papamicael C, Roberts GC, Galleni M, Dideberg O, Frere JM, Schofield CJ. Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols. Org. Biomol. Chem. 6 2008 2282-94 [PubMed: 18563261] http://dx.doi.org/10.1039/b802311e
	Horsfall LE, Garau G, Lienard BM, Dideberg O, Schofield CJ, Frere JM, Galleni M. Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila. Antimicrob. Agents Chemother. 51 2007 2136-42 [PubMed: 17307979] http://dx.doi.org/10.1128/AAC.00866-06
	Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O. Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia. J. Mol. Biol. 375 2008 257-69 [PubMed: 17999929] http://dx.doi.org/10.1016/j.jmb.2007.10.036

InterPro 23.1