ID BLAC_BACCE Reviewed; 306 AA. AC P00809; P70876; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 110. DE RecName: Full=Beta-lactamase 1; DE EC=3.5.2.6; DE AltName: Full=Beta-lactamase I; DE AltName: Full=Penicillinase; DE Flags: Precursor; GN Name=blaY; OS Bacillus cereus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=569/H / NCTC 9945; RX PubMed=6308567; DOI=10.1093/nar/11.14.4997; RA Sloma A., Gross M.; RT "Molecular cloning and nucleotide sequence of the type I beta-lactamase RT gene from Bacillus cereus."; RL Nucleic Acids Res. 11:4997-5004(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=569/H/9; RX PubMed=3124817; DOI=10.1042/bj2480657; RA Madgwick P.J., Waley S.G.; RT "Beta-lactamase I from Bacillus cereus. Structure and site-directed RT mutagenesis."; RL Biochem. J. 248:657-662(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-75. RC STRAIN=569/H / NCTC 9945; RX PubMed=6413253; DOI=10.1016/0014-5793(83)81006-0; RA Mezes P.S.F., Yang Y.Q., Hussain M., Lampen J.O.; RT "Bacillus cereus 569/H beta-lactamase I: cloning in Escherichia coli and RT signal sequence determination."; RL FEBS Lett. 161:195-200(1983). RN [4] RP AMINO ACID NUMBERING SCHEME. RX PubMed=2039479; DOI=10.1042/bj2760269; RA Ambler R.P., Coulson A.F., Frere J.M., Ghuysen J.M., Joris B., Forsman M., RA Levesque R.C., Tiraby G., Waley S.G.; RT "A standard numbering scheme for the class A beta-lactamases."; RL Biochem. J. 276:269-270(1991). CC -!- FUNCTION: This protein is a beta-lactamase with a substrate specificity CC for penicillins. 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 -!- MISCELLANEOUS: The class A beta-lactamase family has a specific amino- CC acid numbering system, sometimes called Ambler or ABL numbering and CC often misspelt as Amber. A multiple sequence alignment was used to CC derive a consensus sequence and then the consensus was numbered taking CC into account insertions and deletions. This allows use of identical CC numbers, e.g. for active site residues, despite differences in protein CC length. UniProt always uses natural numbering of residues, hence there CC appear to be differences in numbering between this entry and some CC papers. {ECO:0000305|PubMed:2039479}. CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA26021.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA29819.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X01990; CAA26021.1; ALT_INIT; Genomic_DNA. DR EMBL; X01602; CAA25753.1; -; Genomic_DNA. DR EMBL; X06599; CAA29819.1; ALT_INIT; Genomic_DNA. DR PIR; A01004; PNBSU. DR AlphaFoldDB; P00809; -. DR SMR; P00809; -. DR BindingDB; P00809; -. DR ChEMBL; CHEMBL5732; -. DR DrugCentral; P00809; -. DR SABIO-RK; P00809; -. 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:InterPro. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 InterPro; IPR058139; BlaC_bacilli. DR NCBIfam; NF033096; bla1; 1. DR NCBIfam; NF033103; bla_class_A; 1. DR NCBIfam; NF012167; classA_firm; 1. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE-TYPE TRANSPEPTIDASE FOLD CONTAINING PROTEIN; 1. DR Pfam; PF13354; Beta-lactamase2; 1. DR PRINTS; PR00118; BLACTAMASEA. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR PROSITE; PS00146; BETA_LACTAMASE_A; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Hydrolase; Signal. FT SIGNAL 1..27 FT CHAIN 28..306 FT /note="Beta-lactamase 1" FT /id="PRO_0000016970" FT ACT_SITE 91 FT /note="Nucleophile; acyl-ester intermediate" FT /evidence="ECO:0000250|UniProtKB:P62593" FT ACT_SITE 94 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P62593" FT ACT_SITE 149 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P62593" FT ACT_SITE 185 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P62593" FT BINDING 253..255 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CONFLICT 273 FT /note="S -> R (in Ref. 2; CAA29819)" FT /evidence="ECO:0000305" FT CONFLICT 278..280 FT /note="VLI -> IAIL (in Ref. 2; CAA29819)" FT /evidence="ECO:0000305" FT CONFLICT 291..292 FT /note="ND -> DN (in Ref. 2; CAA29819)" FT /evidence="ECO:0000305" FT CONFLICT 305..306 FT /note="GS -> ALR (in Ref. 2; CAA29819)" FT /evidence="ECO:0000305" SQ SEQUENCE 306 AA; 33322 MW; F00F4DB9DB6D41AA CRC64; MILKNKRMLK IGICVGILGL SITSLEAFTG ESLQVEAKEK TGQVKHKNQA THKEFSQLEK KFDARLGVYA IDTGTNQTIS YRPNERFAFA STYKALAAGV LLQQNSIDSL NEVITYTKED LVDYSPVTEK HVDTGMKLGE IAEAAVRSSD NTAGNILFNK IGGPKGYEKA LRHMGDRITM SNRFETELNE AIPGDIRDTS TAKAIATNLK AFTVGNALPA EKRKILTEWM KGNATGDKLI RAGIPTDWVV GDKSGAGSYG TRNDIAVVWP PNSAPIIVLI SSKDEKEAIY NDQLIAEATK VIVKGS //