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InterPro: IPR012338 Beta-lactamase-type transpeptidase fold

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UniProtKB
Matches:
25912 proteins
AccessionHelp
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IPR012338 B-lactamase-typ_transpept_fold
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Children IPR001460 Penicillin-binding protein, transpeptidase
IPR001967 Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
IPR015868 Glutaminase, core
Found in IPR000667 Peptidase S13, D-Ala-D-Ala carboxypeptidase C
IPR000871 Beta-lactamase, class A/D
IPR001466 Beta-lactamase-related
Contains IPR001586 Beta-lactamase, class C active site
IPR002137 Beta-lactamase, class D active site
IPR018044 Peptidase S11, D-alanyl-D-alanine carboxypeptidase, conserved region
InterPro annotation
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AbstractHelp
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This entry represents a beta-lactamase structural motif, which contins a cluster of alpha-helices and an alpha/beta sandwich. In addition to beta-lactamases, this domain is also found in D-ala carboxypeptidase/transpeptidase, esterase (EstB) [1], the penicillin receptor BlaR (C-terminal domain), D-aminopeptidase (N-terminal domain) [2], penicillin-biding proteins (e.g. PBP2x, PBP5), and in glutaminase (GlnA). Beta-lactamases are the most common bacterial resistance mechanism against beta-lactam antibiotics [3]. Beta-lactamases appear to have evolved from DD-transpeptidases, which are penicillin-binding proteins involved in cell wall biosynthesis, and as such are one of the main targets of beta-lactam antibiotics.

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1alq , 1axb , 1blc , 1blh , 1blp , 1bls , 1bsg , 1bt5 , 1btl , 1bue , 1bul , 1bza , 1c3b , 1cef , 1ceg , 1ci8 , 1ci9 , 1ck3 , 1dja , 1djb , 1djc , 1dy6 , 1e25 , 1e3u , 1e4d , 1ei5 , 1erm , 1ero , 1erq , 1es2 , 1es3 , 1es4 , 1es5 , 1esi , 1esu , 1ewz , 1fcm , 1fcn , 1fco , 1fof , 1fqg , 1fr1 , 1fr6 , 1fsw , 1fsy , 1g68 , 1g6a , 1ga0 , 1ga9 , 1gce , 1ghi , 1ghm , 1ghp , 1h5x , 1h8y , 1h8z , 1hd8 , 1htz , 1hvb , 1hzo , 1i2s , 1i2w , 1i5q , 1iel , 1iem , 1ikg , 1iki , 1iyo , 1iyp , 1iyq , 1iys , 1j9m , 1jtd , 1jtg , 1jvj , 1jwp , 1jwv , 1jwz , 1k25 , 1k38 , 1k4e , 1k4f , 1k54 , 1k55 , 1k56 , 1k57 , 1k6r , 1k6s , 1kds , 1kdw , 1ke0 , 1ke3 , 1ke4 , 1kge , 1kgf , 1kgg , 1kvl , 1kvm , 1l0d , 1l0e , 1l0f , 1l0g , 1l2s , 1lhy , 1li0 , 1li9 , 1ll5 , 1ll9 , 1llb , 1m40 , 1m6k , 1mbl , 1mki , 1mpl , 1mwr , 1mws , 1mwt , 1mwu , 1mxo , 1my8 , 1n4o , 1n9b , 1nj4 , 1nrf , 1nxy , 1ny0 , 1nym , 1nyy , 1nzo , 1nzu , 1o07 , 1o7e , 1ome , 1ong , 1onh , 1pi4 , 1pi5 , 1pio , 1pmd , 1pw1 , 1pw8 , 1pwc , 1pwd , 1pwg , 1pyy , 1pzo , 1pzp , 1q2p , 1q2q , 1qme , 1qmf , 1rcj , 1rgy , 1rgz , 1rp5 , 1s0w , 1s6r , 1scw , 1sde , 1sdn , 1shv , 1skf , 1tdg , 1tdl , 1tem , 1tvf , 1u60 , 1vm1 , 1vqq , 1w5d , 1w79 , 1w7f , 1w8q , 1w8y , 1we4 , 1wyb , 1wyc , 1xa1 , 1xa7 , 1xgi , 1xgj , 1xkz , 1xp4 , 1xpb , 1xx2 , 1xxm , 1y54 , 1ylj , 1ylp , 1ylt , 1ylw , 1yly , 1ylz , 1ym1 , 1yms , 1ymx , 1yqs , 1yt4 , 1z6f , 1zc2 , 1zg4 , 1zg6 , 1zkj , 2a3u , 2a49 , 2b5r , 2bg1 , 2blm , 2bls , 2c5w , 2c6w , 2cc1 , 2dcf , 2dns , 2drw , 2efu , 2efx , 2ex2 , 2ex6 , 2ex8 , 2ex9 , 2exa , 2exb , 2fff , 2ffy , 2g2u , 2g2w , 2gdn , 2h0t , 2h0y , 2h10 , 2h5s , 2hdq , 2hdr , 2hds , 2hdu , 2hp5 , 2hp6 , 2hp9 , 2hpb , 2i72 , 2iwb , 2iwc , 2iwd , 2j9p , 2jc7 , 2olu , 2olv , 2osu , 2ov5 , 2p74 , 2p9v , 2pby , 2pu2 , 2pu4 , 2q9m , 2q9n , 2qz6 , 2r9w , 2r9x , 2rcx , 2uwx , 2z2l , 2z2m , 2zc3 , 2zc4 , 2zd8 , 3b3x , 3beb , 3bec , 3bfc , 3bfd , 3bfe , 3bff , 3bfg , 3blm , 3bls , 3brm , 3c4o , 3c4p , 3c7u , 3c7v , 3dwk , 3pte , 4blm
SCOP: e.3.1.1 , e.3.1.2 , e.3.1.3

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Overlapping InterPro entriesHelp
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IPR012338 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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A5U493 Beta-lactamase

O94925 Glutaminase kidney isoform, mitochondrial

P73903 Glutaminase

Q09621 Beta-lactamase domain-containing protein 2

Q571F8 Glutaminase liver isoform, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR015868 Glutaminase, core
IPR007043 Glutaminase
IPR002110 Ankyrin repeat
IPR020683 Ankyrin repeat-containing domain
IPR001466 Beta-lactamase-related
IPR012338 Beta-lactamase-type transpeptidase fold
IPR000871 Beta-lactamase, class A/D
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
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1. Wagner UG, Petersen EI, Schwab H, Kratky C.
EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.
Protein Sci. 11 467-78 2002 [PubMed: 11847270]
http://dx.doi.org/10.1110/ps.33002
2. Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J.
Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.
Structure 8 971-80 2000 [PubMed: 10986464]
http://dx.doi.org/10.1016/S0969-2126(00)00188-X
3. Oliva M, Dideberg O, Field MJ.
Understanding the acylation mechanisms of active-site serine penicillin-recognizing proteins: a molecular dynamics simulation study.
Proteins 53 88-100 2003 [PubMed: 12945052]
http://dx.doi.org/10.1002/prot.10450

Additional ReadingHelp
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Michaux C, Massant J, Kerff F, Frere JM, Docquier JD, Vandenberghe I, Samyn B, Pierrard A, Feller G, Charlier P, Van Beeumen J, Wouters J.
Crystal structure of a cold-adapted class C beta-lactamase.
FEBS J. 275 2008 1687-97 [PubMed: 18312599]
http://dx.doi.org/10.1111/j.1742-4658.2008.06324.x
Nukaga M, Bethel CR, Thomson JM, Hujer AM, Distler A, Anderson VE, Knox JR, Bonomo RA.
Inhibition of class A beta-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1.
J. Am. Chem. Soc. 130 2008 12656-62 [PubMed: 18761444]
http://dx.doi.org/10.1021/ja7111146
Brown G, Singer A, Proudfoot M, Skarina T, Kim Y, Chang C, Dementieva I, Kuznetsova E, Gonzalez CF, Joachimiak A, Savchenko A, Yakunin AF.
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.
Biochemistry 47 2008 5724-35 [PubMed: 18459799]
http://dx.doi.org/10.1021/bi800097h
Wang J, Palzkill T, Chow DC.
Structural insight into the kinetics and DeltaCp of interactions between TEM-1 beta-lactamase and beta-lactamase inhibitory protein (BLIP).
J. Biol. Chem. 284 2009 595-609 [PubMed: 18840610]
http://dx.doi.org/10.1074/jbc.M804089200
Sauvage E, Powell AJ, Heilemann J, Josephine HR, Charlier P, Davies C, Pratt RF.
Crystal structures of complexes of bacterial DD-peptidases with peptidoglycan-mimetic ligands: the substrate specificity puzzle.
J. Mol. Biol. 381 2008 383-93 [PubMed: 18602645]
http://dx.doi.org/10.1016/j.jmb.2008.06.012
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