ID B1PZ97_ECOLX Unreviewed; 381 AA.
AC B1PZ97;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=blaCMY-40 {ECO:0000313|EMBL:ACA30422.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACA30422.1};
RN [1] {ECO:0000313|EMBL:ACA30422.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N2301 {ECO:0000313|EMBL:ACA30422.1};
RX PubMed=19523051; DOI=10.1111/j.1469-0691.2009.02864.x;
RA Mata C., Miro E., Rivera A., Mirelis B., Coll P., Navarro F.;
RT "Prevalence of acquired AmpC beta-lactamases in Enterobacteriaceae lacking
RT inducible chromosomal ampC genes at a Spanish hospital from 1999 to 2007.";
RL Clin. Microbiol. Infect. 16:472-476(2010).
CC -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC specificity for cephalosporins. {ECO:0000256|ARBA:ARBA00003808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; EU515251; ACA30422.1; -; Genomic_DNA.
DR RefSeq; WP_063859840.1; NG_048835.1.
DR AlphaFoldDB; B1PZ97; -.
DR SMR; B1PZ97; -.
DR MEROPS; S12.006; -.
DR KEGG; ag:ACA30422; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..381
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002768666"
FT DOMAIN 32..380
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 381 AA; 42016 MW; 06D90C1AF7C53ABA CRC64;
MMKKSLCCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV AVIYQGKPYY
FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDAIAR GEIKLSDPVT KYWPELTGKQ
WQGISLLHLA TYTAGGLPLQ IPDDVTDKAA LLRFYQNWQP QWTPGAKRLY ANSSIGLFGT
LAVKPSGMSY EEAMTRRVLQ PLKLAHTWIT VPQSEQKDYA WGYREGKPVH VSPGQLDAEA
YGVKSSVIDM AHWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA
DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGYTG GFGSYVAFVP EKNLGIVMLA
NKSYPNPVRV EAAWRILEKL Q
//
