ID   AMPC_SERMA              Reviewed;         376 AA.
AC   P18539;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
GN   Name=ampC;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr50;
RX   PubMed=2227364; DOI=10.1111/j.1574-6968.1990.tb13992.x;
RA   Nomura K., Yoshida T.;
RT   "Nucleotide sequence of the Serratia marcescens SR50 chromosomal ampC beta-
RT   lactamase gene.";
RL   FEMS Microbiol. Lett. 58:295-299(1990).
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; X52964; CAA37137.1; -; Genomic_DNA.
DR   PIR; A48176; QKSE.
DR   AlphaFoldDB; P18539; -.
DR   SMR; P18539; -.
DR   STRING; 273526.SMDB11_1530; -.
DR   ChEMBL; CHEMBL5693; -.
DR   MEROPS; S12.006; -.
DR   SABIO-RK; P18539; -.
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   CHAIN           22..376
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016965"
FT   ACT_SITE        79
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         328..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41096 MW;  890CEE7C27925150 CRC64;
     MTKMNRCAAL IAALILPTAH AAQQQDIDAV IQPLMKKYGV PGMAIAVSVD GKQQIYPYGV
     ASKQTGKPIT EQTLFEVGSL SKTFTATLAV YAQQQSKLSF KDPASHYLPD VRGSAFDGVS
     LLNLATHTSG LPLFVPDDVT NNAQLMAYYR AWQPKHPAGS YRVYSNLGIG MLGMIAAKSL
     DQPFIQAMEQ GMLPALGMSH TYVQVPAAQM ANYAQGYSKD DKPVRVNPGP LDAESYGIKS
     NARDLIRYLD ANLQQVKVAS VARRWPRRTS VITSAGAFTQ DLMWENYPYP VKLSRLIEGN
     NAGMIMNGTP ATAITPPQPE LRAGWYNKTG STGGFSTYAV FIPAKNIAVE MLANKWFPND
     DRVEAAYHII QALEKR