ID BLAC_STRCE Reviewed; 311 AA. AC Q06650; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 87. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Penicillinase; DE Flags: Precursor; GN Name=bla; OS Streptomyces cellulosae. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1968; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KCC S0127; RX PubMed=7916705; DOI=10.1016/0378-1119(93)90769-y; RA Ogawara H.; RT "Sequence of a gene encoding beta-lactamase from Streptomyces cellulosae."; RL Gene 124:111-114(1993). CC -!- FUNCTION: Hydrolyzes benzylpenicillin and cloxacillin (at 10% of the CC rate of benzylpenicillin). 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 -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family. CC {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; D12653; BAA02176.1; -; Genomic_DNA. DR PIR; JN0520; JN0520. DR AlphaFoldDB; Q06650; -. DR SMR; Q06650; -. 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; 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; IPR006311; TAT_signal. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-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. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Hydrolase; NADP; Signal. FT SIGNAL 1..36 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648" FT CHAIN 37..311 FT /note="Beta-lactamase" FT /id="PRO_0000017015" FT ACT_SITE 86 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101" FT BINDING 252..254 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 311 AA; 33137 MW; F3578EBEEA92A3FB CRC64; MRKPTSSLTR RSVLGAGLGL GGALALGSTT ASAASAGTTP SENPAAVRRL RALEREHQAR IGVFALNLAT GASLLHRAHE LFPMCSVFKT LAAAAVLRDL DHDGSQLARV IRYTEADVTK SGHAPVTKDH IDTGMTIRDL CDATIRYSDN CAANLLLREL GGPTAVTRFC RSLGDPVTRL DRWEPELNSG EPDRRTDTTS PYAIARTYQR LVLGNALNRP DRALLTDWLL RNTTTLTTFR TGLPKGWTVA DKSGGGDTYG TRNEAAIAWT PDGAPVLLTA LTHKPSLPTA PGDTPLIIKL ATVLSEAVAP A //