ID   BLA1_STRCI              Reviewed;         325 AA.
AC   Q03680;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Beta-lactamase 1;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=blaL;
OS   Streptomyces cacaoi.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 3082 / DSM 40057 / JCM 4352 / BCRC 12103 / KCC S-0352 /
RC   LMG 19320 / NBRC 12748 / NCIMB 9626 / IMRU 3082;
RA   Lenzini M.V., Ishihara H., Dusart J., Ogawara H., Joris B., Beeumen J.,
RA   Frere J.-M., Ghuysen J.-M.;
RT   "Nucleotide sequence of the gene encoding the active-site serine beta-
RT   lactamase from Streptomyces cacaoi.";
RL   FEMS Microbiol. Lett. 49:371-376(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=ATCC 3082 / DSM 40057 / JCM 4352 / BCRC 12103 / KCC S-0352 /
RC   LMG 19320 / NBRC 12748 / NCIMB 9626 / IMRU 3082;
RX   PubMed=2228966; DOI=10.1128/jb.172.11.6427-6434.1990;
RA   Urabe H., Lenzini M.V., Mukaide M., Dusart J., Nakano M.M., Ghuysen J.-M.,
RA   Ogawara H.;
RT   "Beta-lactamase expression in Streptomyces cacaoi.";
RL   J. Bacteriol. 172:6427-6434(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 89-96, AND ACTIVE SITE SER-93.
RX   PubMed=2822004; DOI=10.1042/bj2440427;
RA   de Meester F., Joris B., Lenzini M.V., Dehottay P., Erpicium T., Dusart J.,
RA   Klein D., Ghuysen J.-M., Frere J.-M., van Beeumen J.;
RT   "The active sites of the beta-lactamases of Streptomyces cacaoi and
RT   Streptomyces albus G.";
RL   Biochem. J. 244:427-432(1987).
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).
RN   [5]
RP   COMPARISON OF BLAU AND BLAL.
RX   PubMed=1468613; DOI=10.1016/0378-1097(92)90295-y;
RA   Magdalena J., Forsman M., Lenzini M.V., Brans A., Dusart J.;
RT   "Two different beta-lactamase genes are present in Streptomyces cacaoi.";
RL   FEMS Microbiol. Lett. 78:101-105(1992).
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}.
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DR   EMBL; D90201; BAA14224.1; -; Genomic_DNA.
DR   PIR; A37148; A37148.
DR   RefSeq; WP_065102178.1; NG_050939.1.
DR   AlphaFoldDB; Q03680; -.
DR   SMR; Q03680; -.
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   NCBIfam; NF033103; bla_class_A; 1.
DR   NCBIfam; NF033101; blaL; 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   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..325
FT                   /note="Beta-lactamase 1"
FT                   /id="PRO_0000017016"
FT   REGION          30..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101,
FT                   ECO:0000269|PubMed:2822004"
FT   BINDING         270..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  34758 MW;  8E328575B353ABA3 CRC64;
     MRIRPTRRLL LGAVAPLALV PLVACGQASG SESGQQPGLG GCGTSAHGSA DAHEKEFRAL
     EKKFDAHPGV YAIDTRDGQE ITHRADERFA YGSTFKALQA GAILAQVLRD GREVRRGAEA
     DGMDKVVHYG QDAILPNSPV TEKHVADGMS LRELCDAVVA YSDNTAANLL FDQLGGRRGS
     TRVLKQLGDH TTSMDRYEQE LGSAVPGDPR DTSTPRAFAE DLRAFAVEDG EKAALAPNDR
     EQLNDWMSGS RTGDALIRAG VPKDWKVEDK SGQVKYGTRN DIAVVRPPGR APIVVSVMSH
     GDTQDAEPHD ELVAEAGLVV ADGLK
//