ID   Q14F43_ECOLX            Unreviewed;       175 AA.
AC   Q14F43;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE   Flags: Fragment;
GN   Name=ampC {ECO:0000313|EMBL:AAY89684.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:AAY89684.1};
RN   [1] {ECO:0000313|EMBL:AAY89684.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LW1655F+ {ECO:0000313|EMBL:AAY89684.1};
RA   Siddiqui R.A., Heinze I., Platzer M.;
RT   "Complex mutation pattern in the design of a protoplast type L-form
RT   Escherichia coli.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC       specificity for cephalosporins. {ECO:0000256|ARBA:ARBA00003808}.
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;
CC         Evidence={ECO:0000256|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR   EMBL; AY616621; AAY89684.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q14F43; -.
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-UniRule.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140}.
FT   DOMAIN          23..174
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY89684.1"
FT   NON_TER         175
FT                   /evidence="ECO:0000313|EMBL:AAY89684.1"
SQ   SEQUENCE   175 AA;  19133 MW;  3A7A60A47BC80972 CRC64;
     CALLITASCS TFAAPQQIND IVHRTITPLI EQQKIPGMAV AVIYQGKPYY FTWGYADIAK
     KQPVTQQTLF ELGSVSKTFT GVLGGDAIAR GEIKLSDPTT KYWPELTAKQ WNGITLLHLA
     TYTAGGLPLQ VPDEVKSSSD LLRFYQNWQP AWAPGTQRLY ANSSIGLFGA LAVKP
//