ID   AMPC_LYSLA              Reviewed;         385 AA.
AC   Q48743;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
OS   Lysobacter lactamgenus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=39596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YK90;
RX   PubMed=8703429; DOI=10.1007/bf00172490;
RA   Kimura H., Izawa M., Sumino Y.;
RT   "Molecular analysis of the gene cluster involved in cephalosporin
RT   biosynthesis from Lysobacter lactamgenus YK90.";
RL   Appl. Microbiol. Biotechnol. 44:589-596(1996).
CC   -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC       specificity for cephalosporins.
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:PRU10102};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; X56660; CAA39987.1; -; Genomic_DNA.
DR   PIR; S54103; S54103.
DR   AlphaFoldDB; Q48743; -.
DR   SMR; Q48743; -.
DR   MEROPS; S12.006; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017001; P: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; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..385
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016960"
FT   ACT_SITE        84
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  41878 MW;  33DA95118FC2B207 CRC64;
     MKRLLAFCLL FFAALGQAKV PPPARSAADA EIQRAVAAFM QQYQVPGVAV GITVDGAERY
     YNYGVSSRKT QAKVGANTLF EVGSVSKTFT ATLASYAQVN QQLSLADHPG KYLPEMKGHD
     FDKVTLLNLG THTAGGFPMQ VPTQVKTDQQ LTAYFQSWHP QYPAGTKRTY ANPGIGMLGV
     IAAKSMRMPF QKAMTGVLLP KLGLTNTYLT VPPAKMAFYA QGYDDKGQPV RMSPGALWEP
     TYGIKTTARD LLRFVEINLD QVKVEPKLKR AIDGTHVGYY RLGEMTQGLV WEQLPYPASE
     TSLQANSSQK VIFESNAVAA LTPPRPPQAN VLINKTGSTR GFGAYVAFNP ARKIGIVLLM
     NRSVPMDGRI KLAHTILDTA GGMAK