ID   AMPC_YEREN              Reviewed;         388 AA.
AC   P45460;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
GN   Name=ampC;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IP97 / Serotype O:5B;
RX   PubMed=1510392; DOI=10.1128/aac.36.5.1049;
RA   Seoane A., Francia M.V., Garcia Lobo J.M.;
RT   "Nucleotide sequence of the ampC-ampR region from the chromosome of
RT   Yersinia enterocolitica.";
RL   Antimicrob. Agents Chemother. 36:1049-1052(1992).
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; X63149; CAA44850.1; -; Genomic_DNA.
DR   PIR; B48899; B48899.
DR   RefSeq; WP_020283255.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; P45460; -.
DR   SMR; P45460; -.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..388
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016966"
FT   ACT_SITE        89
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         342..344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43111 MW;  7352BC99129C56DA CRC64;
     MMKKSIINTL IFTSIATFPL YTLAQTKLTE LQVATIVNNT LTPLLEKQGI PGMAVAVFYD
     GKPQFFNYGM ADIKAGRPVT ENTLFELGSV SKTFTGVAGE YAMQTGIMNL NDPVTEYAPE
     LTGSQWKDVK MLHLATYTAG GLPLQLPDSV TDQKSLWQYY QQWQPQWAPG VMRNYSNASI
     GLFGALAVKR SQLTFENYMK EYVFQPLKLD HTFITIPESM QSNYAWGYKD GQPVRVTLGM
     LGEEAYGVKS TSQDMVRFMQ ANMDPESLPA GNDKLKEAII ASQSRYFQAG DMFQGLGWEM
     YSWPINPQGV IADSGNDIAL KPRKVEALVP AQPAVRASWV HKTGATNGFG AYIVFIPEEK
     VGIVMLANKN YPNPVRVQAA YDILQALR