ID Q933M6_ENTCL Unreviewed; 381 AA.
AC Q933M6;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 03-MAY-2023, 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:AAL05855.1};
OS Enterobacter cloacae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550 {ECO:0000313|EMBL:AAL05855.1};
RN [1] {ECO:0000313|EMBL:AAL05855.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K9911729 {ECO:0000313|EMBL:AAL05856.1}, K9914325
RC {ECO:0000313|EMBL:AAL05858.1}, and K99230
RC {ECO:0000313|EMBL:AAL05855.1};
RX PubMed=12791868; DOI=10.1128/JCM.41.6.2477-2482.2003;
RA Lee S.H., Kim J.Y., Shin S.H., An Y.J., Choi Y.W., Jung Y.C., Jung H.I.,
RA Sohn E.S., Jeong S.H., Lee K.J.;
RT "Dissemination of SHV-12 and characterization of new AmpC-type beta-
RT lactamase genes among clinical isolates of enterobacter species in Korea.";
RL J. Clin. Microbiol. 41:2477-2482(2003).
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; AF411146; AAL05855.1; -; Genomic_DNA.
DR EMBL; AF411147; AAL05856.1; -; Genomic_DNA.
DR EMBL; AF411149; AAL05858.1; -; Genomic_DNA.
DR PIR; B60908; B60908.
DR AlphaFoldDB; Q933M6; -.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140, ECO:0000313|EMBL:AAL05855.1};
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_5008429409"
FT DOMAIN 32..380
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 381 AA; 41252 MW; 67912CBE5CBD3C93 CRC64;
MMIKSLCCAL LLGLSCSALA APVSEKQLAE VVANTVTPLM KAQSVPGMAV AVIYQGKPHY
YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR GEISLDDPVT RYWPQLTGKQ
WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS LLRFYQNWQP QWKPGTTRLY ANASIGLFGA
LAVKPSGMPY EQAMTTRVLK PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGTLDAQA
YGVKTNVQDM ANWVMANMAP EKVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA
NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP EKQIGIVMLA
NKSYPNPARV EAAYHILEAL Q
//
