ID   BLA3_BACCE              Reviewed;         316 AA.
AC   P06548;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Beta-lactamase 3;
DE            EC=3.5.2.6;
DE   AltName: Full=Beta-lactamase III;
DE   Flags: Precursor;
GN   Name=blaZ;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 135-146.
RC   STRAIN=569/H / NCTC 9945;
RX   PubMed=3027036; DOI=10.1128/jb.169.2.579-586.1987;
RA   Hussain M., Pastor F.I.J., Lampen J.O.;
RT   "Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a
RT   lipoprotein of Bacillus cereus 569/H.";
RL   J. Bacteriol. 169:579-586(1987).
RN   [2]
RP   DIACYLGLYCEROL AT CYS-30, AND PALMITOYLATION AT CYS-30.
RX   PubMed=6414515; DOI=10.1021/bi00289a007;
RA   Nielsen J.B., Lampen J.O.;
RT   "Beta-lactamase III of Bacillus cereus 569: membrane lipoprotein and
RT   secreted protein.";
RL   Biochemistry 22:4652-4656(1983).
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M15195; AAA22274.1; -; Genomic_DNA.
DR   PIR; A27755; PNBSLC.
DR   AlphaFoldDB; P06548; -.
DR   SMR; P06548; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Direct protein sequencing; Hydrolase;
KW   Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..29
FT   CHAIN           30..316
FT                   /note="Beta-lactamase 3"
FT                   /id="PRO_0000016968"
FT   REGION          34..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         257..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   LIPID           30
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:6414515"
FT   LIPID           30
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:6414515"
SQ   SEQUENCE   316 AA;  35141 MW;  27A082AB9CCBC9DF CRC64;
     MFVLNKFFTN SHYKKIVPVV LLSCATLIGC SNSNTQSESN KQTNQTNQVK QENKRNHAFA
     KLEKEYNAKL GIYALDTSTN QTVAYHADDR FAFASTSKSL AVGALLRQNS IEALDERITY
     TRKDLSNYNP ITEKHVDTGM TLKELADASV RYSDSTAHNL ILKKLGGPSA FEKILREMGD
     TVTNSERFEP ELNEVNPGET HDTSTPKAIA KTLQSFTLGT VLPSEKRELL VDWMKRNTTG
     DKLIRAGVPK GWEVADKTGA GSYGTRNDIA IIWPPNKKPI VLSILSNHDK EDAEYDDTLI
     ADATKIVLET LKVTNK