ID Q8RML4_9ENTR Unreviewed; 381 AA.
AC Q8RML4;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 72.
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};
GN Name=ampC {ECO:0000313|EMBL:AAM11666.1};
OS Enterobacter cancerogenus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=69218 {ECO:0000313|EMBL:AAM11666.1};
RN [1] {ECO:0000313|EMBL:AAM11666.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12393205;
RA Naas T., Aubert D., Fortineau N., Nordmann P.;
RT "Cloning and sequencing of the beta-lactamase gene and surrounding DNA
RT sequences of Citrobacter braakii, Citrobacter murliniae, Citrobacter
RT werkmanii, Escherichia fergusonii and Enterobacter cancerogenus.";
RL FEMS Microbiol. Lett. 215:81-87(2002).
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; AF492446; AAM11666.1; -; Genomic_DNA.
DR RefSeq; WP_006178946.1; NZ_QGAL01000004.1.
DR AlphaFoldDB; Q8RML4; -.
DR SMR; Q8RML4; -.
DR MEROPS; S12.006; -.
DR KEGG; ecan:CWI88_20280; -.
DR PATRIC; fig|69218.4.peg.4173; -.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..381
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014312302"
FT DOMAIN 32..380
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 381 AA; 41357 MW; ACB32217AEDAC11C CRC64;
MKKKLVFCAL LLGVSCSALA SSLSEKELAK VVKRTVTPLM KAQSIPGMAV AVIYQGQPHY
FTFGKADVAA NTPVTPQTLF ELGSVSKTFT GVLGGDAIAR GEISLNDPVT RYWPELTGKQ
WQGIRLLDLA TYTAGGLPLQ VPDNVTDPAA LLNFYQTWQP QWKPGTTRLY ANSSIGLFGA
LAVKPSGMGF EQAMTTRVLK PLKLDHTWIQ VPKSEEQHYA WGYRDGKAVH VSPGMLDGEA
YGVKSNAEDM ASWVMVNMAP ERVQATSLKQ GIALAQSRYW RVGSMYQGLG WEMLNWPVDG
KTIIDGSDNK IALAALPARE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP EKQLGIVMLA
NKSYPNPARV EAAYQILNAL Q
//
