ID   AMPC_PROST              Reviewed;         384 AA.
AC   O69773;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-MAY-2023, entry version 82.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
GN   Name=ampC;
OS   Providencia stuartii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VDG 96;
RA   Koeck J.L., Basmaciogullari S., Parzy D., Barnaud G., Teyssou R.,
RA   Buisson Y., Philippon A., Arlet G.J.;
RT   "Cloning and sequencing of ampC and ampR genes from Providencia stuartii.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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; Y17315; CAA76739.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69773; -.
DR   SMR; O69773; -.
DR   STRING; 588.BGK56_12160; -.
DR   ChEMBL; CHEMBL5895; -.
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; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..384
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016962"
FT   ACT_SITE        87
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         337..339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   384 AA;  43366 MW;  8CCCAC7F9B1377E9 CRC64;
     MDNSMKNIFR QGRLFIALSL AMTSISAFAL TQQEVDDIIK PLMKQEQIPG MSVAISVNGK
     QAIYHYGVQS KQTQIPVSDR TLYEIGSLSK TFTATLATYA QIQGKLDFSQ SVSHYLPELK
     GSAFDNVSVM NLATHTSGLS LFVPSDIKTN DQLMAYYQKW LPDNEVGQYR SYSNLGVGLL
     GIVTAKQLNM PFSQAMEKLM LPSLGLKHTY IHVPKSQEKY YAQGYNKQNQ PVRLNLEILG
     PEAYGLKSNA KDLIRYLEIN MQSIKVAKTW QEAIENTHTG VYLTDSFVQD MMWESYPWPV
     SLSQLLQGNR DDMALKPQKV ELIKPAMAPE VRAYYNKTGS SNGFATYAIF IPEEKIAIVM
     LSNKWIPIPQ RITATYQLLE KIER
//