ID   AMPC_MORMO              Reviewed;         379 AA.
AC   P94958;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, 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   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SLM01;
RX   PubMed=9066104; DOI=10.1111/j.1574-6968.1997.tb10260.x;
RA   Barnaud G., Arlet G., Danglot C., Philippon A.;
RT   "Cloning and sequencing of the gene encoding the AmpC beta-lactamase of
RT   Morganella morganii.";
RL   FEMS Microbiol. Lett. 148:15-20(1997).
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; Y10283; CAA71326.1; -; Genomic_DNA.
DR   RefSeq; WP_063860105.1; NG_049067.1.
DR   AlphaFoldDB; P94958; -.
DR   SMR; P94958; -.
DR   STRING; 582.AL531_12210; -.
DR   BindingDB; P94958; -.
DR   ChEMBL; CHEMBL5764; -.
DR   DrugCentral; P94958; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..379
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016961"
FT   ACT_SITE        83
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         333..335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  41272 MW;  2A6BA5C3B1862873 CRC64;
     MKKSLSATLI SALLAFSAPG FSAADNVAAV VDSTIKPLMA QQDIPGMAVA VSVKGKPYYF
     NYGFADVQAK QPVTENTLFE LGSVSKTFTG VLGAVSVAKK EMTLNDPAEK YQPELALPQW
     KGITLLDLAT YTAGGLPLQV PDAVKSRADL LHFYQQWQPS RKPGDMRLYA NSSIGLFGAL
     TANAAGMPYE QLLTARILAP LGLSHTFITV PESAQSQYAY GYKNKKPVRV SPGQLDAESY
     GVKSASKDML RWAEMNMEPS RAGNADLEMA MYLAQTRYYK TAAINQGLGW EMYDWPQQKD
     MIINGVTNEV ALQPHPVTDN QVQPYNRASW VHKTGATTGF GAYVAFIPEK QVAIVILANK
     NYPNTERVKA AQAILSALE