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InterPro: IPR001460 Penicillin-binding protein, transpeptidase

Protein matches Help

UniProtKB

Matches:

11113 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

IPR001460 PCN-bd_Tpept

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00905	Transpeptidase	11113
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012338 Beta-lactamase-type transpeptidase fold

Found in

IPR011813 Penicillin-binding protein 1B
IPR011815 Penicillin-binding protein 1C
IPR011816 Penicillin-binding protein 1A
IPR011927 Stage V sporulation protein D
IPR017790 Penicillin-binding protein 2

Contains

IPR002137 Beta-lactamase, class D active site

GO Term annotation Help

Process

GO:0009273 peptidoglycan-based cell wall biogenesis

Function

GO:0008658 penicillin binding

InterPro annotation

Entry Details in BioMart

Abstract

This signature identifies a large group of proteins, which include:

Beta-lactamase precursor (EC:3.5.2.6, penicillinase)
Peptidoglycan synthetase ftsI (EC:2.4.1.129, peptidoglycan glycosyltransferase 3)
Methicillin resistance mecR1 protein
Methicillin resistance blaR1 protein

The large number of penicillin binding proteins, which are represented in this group of sequences, are responsible for the final stages of peptidoglycan biosynthesis for cell wall formation. The proteins synthesise cross-linked peptidoglycan from lipid intermediates, and contain a penicillin-sensitive transpeptidase carboxy-terminal domain. The active site serine (residue 337 in P14677) is conserved in all members of this family [1].

MecR1 and BlaR1 are metallopeptidases belonging to MEROPS peptidase family M56, clan M-. BlaR1 and MecR1 cleave their cognate transcriptional repressors BlaI and MecI, respectively, activating the synthesis of MecA.

MecR1 is present in Staphylococcus aureus and Staphylococcus sciuri, whereas BlaR1 (also known as BlaR, PenR1, or PenJ) has been found in Bacillus licheniformis, Staphylococcus epidermidis, Staphylococcus haemolyticus, and several S. aureus strains. These proteins are either plasmid-encoded, chromosomal, or transposon-mediated. MecR1/BlaR1 proteins are made up by homologous N-terminal 330-residue transmembrane metallopeptidase domains linked to extracellular 260-residue homologous PBP-like penicillin sensor moieties.

Structural links Help

PDB - click here

SCOP: e.3.1.1

CATH: 3.40.710.10

Database links Help

PANDIT: PF00905

Blocks: IPB001460

MEROPS: M56

Pfam Clan: CL0013.14

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001460

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2CI41 Peptidoglycan synthetase ftsI homolog

O66874 Penicillin-binding protein 1A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011816	Penicillin-binding protein 1A
IPR001264	Glycosyl transferase, family 51
IPR005311	Penicillin-binding protein, dimerisation domain
IPR001460	Penicillin-binding protein, transpeptidase
IPR012338	Beta-lactamase-type transpeptidase fold
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3 284-9 1996 [PubMed: 8605631] http://dx.doi.org/10.1038/nsb0396-284

Additional Reading Open in usermanual
	Yamada M, Watanabe T, Baba N, Takeuchi Y, Ohsawa F, Gomi S. Crystal structures of biapenem and tebipenem complexed with penicillin-binding proteins 2X and 1A from Streptococcus pneumoniae. Antimicrob. Agents Chemother. 52 2008 2053-60 [PubMed: 18391040] http://dx.doi.org/10.1128/AAC.01456-07
	Yamada M, Watanabe T, Miyara T, Baba N, Saito J, Takeuchi Y, Ohsawa F. Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity. Antimicrob. Agents Chemother. 51 2007 3902-7 [PubMed: 17724158] http://dx.doi.org/10.1128/AAC.00743-07
	Lovering AL, de Castro LH, Lim D, Strynadka NC. Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science 315 2007 1402-5 [PubMed: 17347437] http://dx.doi.org/10.1126/science.1136611
	Lovering AL, De Castro L, Strynadka NC. Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer. J. Mol. Biol. 383 2008 167-77 [PubMed: 18760285] http://dx.doi.org/10.1016/j.jmb.2008.08.020
	Santillana E, Beceiro A, Bou G, Romero A. Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis. Proc. Natl. Acad. Sci. U.S.A. 104 2007 5354-9 [PubMed: 17374723] http://dx.doi.org/10.1073/pnas.0607557104

InterPro 23.1