ID Q44219_AERSO Unreviewed; 382 AA.
AC Q44219;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, 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};
OS Aeromonas sobria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=646 {ECO:0000313|EMBL:AAA83416.1};
RN [1] {ECO:0000313|EMBL:AAA83416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AER 14 {ECO:0000313|EMBL:AAA83416.1};
RX PubMed=7811022;
RA Rasmussen B.A., Keeney D., Yang Y., Bush K.;
RT "Cloning and expression of a cloxacillin-hydrolyzing enzyme and a
RT cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli:
RT requirement for an E. coli chromosomal mutation for efficient expression of
RT the class D enzyme.";
RL Antimicrob. Agents Chemother. 38:2078-2085(1994).
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; U10250; AAA83416.1; -; Genomic_DNA.
DR PIR; I39695; I39695.
DR RefSeq; WP_063840463.1; NG_047381.1.
DR AlphaFoldDB; Q44219; -.
DR SMR; Q44219; -.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..382
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004232046"
FT DOMAIN 33..379
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 382 AA; 40742 MW; 051B28B06FEE6BB5 CRC64;
MKQPTTLSLL TLGSLLISSF ASAAQDAPLT AIVDGAIQPV LKEYRIPGMA VAVLKDGKAH
YFNYGVANRE SGQRVSEQTL FEIGSVSKTY TSTLGAYAVV KGGFKLDDKV SRHAPWLKGS
AFDGITMAEL ATYSAGGLPL QFPDEVESVE QMQAYYRQWT PAYQPGSHRQ YSNPSIGLFG
YLAASSLGQP FEQLMSQTLL PGLALLPTPT SRCLRGMGDY AYGCAKEEKP IRVNPGVLAD
EAYGIKTSSA DLLAFVKANI SGVDDKALQQ AISLTHQGRY SVGEMTQGLG WESYAYPVSE
QTLLAGNSSA VIYNANPVKP VAASQETGGA RLYNKTGSTN GFGAYVAFVP AKGIGIVMLA
NRNYPNDARV KAAYAILSKL AD
//
